Skip to main content
Bacteriological Reviews logoLink to Bacteriological Reviews
. 1972 Mar;36(1):109–134. doi: 10.1128/br.36.1.109-134.1972

Translation of the genome of a ribonucleic acid bacteriophage.

M Kozak, D Nathans
PMCID: PMC378432  PMID: 4555183

Full text

PDF
109

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adams J. M., Capecchi M. R. N-formylmethionyl-sRNA as the initiator of protein synthesis. Proc Natl Acad Sci U S A. 1966 Jan;55(1):147–155. doi: 10.1073/pnas.55.1.147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Adams J. M., Cory S. Untranslated nucleotide sequence at the 5'-end of R17 bacteriophage RNA. Nature. 1970 Aug 8;227(5258):570–574. doi: 10.1038/227570a0. [DOI] [PubMed] [Google Scholar]
  3. August J. T. Mechanism of synthesis of bacteriophage RNA. Nature. 1969 Apr 12;222(5189):121–123. doi: 10.1038/222121a0. [DOI] [PubMed] [Google Scholar]
  4. BRINTON C. C., Jr, GEMSKI P., Jr, CARNAHAN J. A NEW TYPE OF BACTERIAL PILUS GENETICALLY CONTROLLED BY THE FERTILITY FACTOR OF E. COLI K 12 AND ITS ROLE IN CHROMOSOME TRANSFER. Proc Natl Acad Sci U S A. 1964 Sep;52:776–783. doi: 10.1073/pnas.52.3.776. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Becarevic A., Naono S., Lelong J. -C., Gros F. Formation of initiation complex with lambdamRNA in vitro. FEBS Lett. 1970 Dec 18;11(5):312–315. doi: 10.1016/0014-5793(70)80556-7. [DOI] [PubMed] [Google Scholar]
  6. Berissi H., Groner Y., Revel M. Effect of a purified initiation factor F3 (B) on the selection of ribosomal binding sites on phage MS2 RNA. Nat New Biol. 1971 Nov 10;234(45):44–47. doi: 10.1038/newbio234044a0. [DOI] [PubMed] [Google Scholar]
  7. Billeter M. A., Dahlberg J. E., Goodman H. M., Hindley J., Weissmann C. Sequence of the first 175 nucleotides from the 5' terminus of Qbeta RNA synthesized in vitro. Nature. 1969 Dec 13;224(5224):1083–1086. doi: 10.1038/2241083a0. [DOI] [PubMed] [Google Scholar]
  8. Billeter M. A., Libonati M., Viñuela E., Weissmann C. Replication of viral ribonucleic acid. X. Turnover of virus-specific double-stranded ribonucleic acid during replication of phage MS2 in Escherichia coli. J Biol Chem. 1966 Oct 25;241(20):4750–4757. [PubMed] [Google Scholar]
  9. Bretscher M. S. Polypeptide chain termination: an active process. J Mol Biol. 1968 May 28;34(1):131–136. doi: 10.1016/0022-2836(68)90239-8. [DOI] [PubMed] [Google Scholar]
  10. Capecchi M. R. Cell-free protein synthesis programmed with R17 RNA: identification of two phage proteins. J Mol Biol. 1966 Oct 28;21(1):173–193. doi: 10.1016/0022-2836(66)90086-6. [DOI] [PubMed] [Google Scholar]
  11. Capecchi M. R., Gussin G. N. Suppression in vitro: Identification of a Serine-sRNA as a "Nonsense" Suppressor. Science. 1965 Jul 23;149(3682):417–422. doi: 10.1126/science.149.3682.417. [DOI] [PubMed] [Google Scholar]
  12. Capecchi M. R., Klein H. A. Characterization of three proteins involved in polypeptide chain termination. Cold Spring Harb Symp Quant Biol. 1969;34:469–477. doi: 10.1101/sqb.1969.034.01.053. [DOI] [PubMed] [Google Scholar]
  13. Capecchi M. R., Klein H. A. Release factors mediating termination of complete proteins. Nature. 1970 Jun 13;226(5250):1029–1033. doi: 10.1038/2261029a0. [DOI] [PubMed] [Google Scholar]
  14. Capecchi M. R. Polarity in vitro. J Mol Biol. 1967 Nov 28;30(1):213–217. doi: 10.1016/0022-2836(67)90254-9. [DOI] [PubMed] [Google Scholar]
  15. Capecchi M. R. Polypeptide chain termination in vitro: isolation of a release factor. Proc Natl Acad Sci U S A. 1967 Sep;58(3):1144–1151. doi: 10.1073/pnas.58.3.1144. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Carter T., Newton A. New polarity suppressors in Escherichia coli: suppression and messenger RNA stability. Proc Natl Acad Sci U S A. 1971 Dec;68(12):2962–2966. doi: 10.1073/pnas.68.12.2962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Caskey C. T., Beaudet A. L., Scolnick E. M., Rosman M. Hydrolysis of fMet-tRNA by peptidyl transferase. Proc Natl Acad Sci U S A. 1971 Dec;68(12):3163–3167. doi: 10.1073/pnas.68.12.3163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Caskey T., Scolnick E., Tompkins R., Goldstein J., Milman G. Peptide chain termination, codon, protein factor, and ribosomal requirements. Cold Spring Harb Symp Quant Biol. 1969;34:479–488. doi: 10.1101/sqb.1969.034.01.054. [DOI] [PubMed] [Google Scholar]
  19. Contreras R., Vandenberghe A., Jou W. Min, De Wachter R., Fiers W. Studies on the bacteriophage MS2 nucleotide sequence of a 3'-terminal fragment (n = 104). FEBS Lett. 1971 Oct 15;18(1):141–144. doi: 10.1016/0014-5793(71)80430-1. [DOI] [PubMed] [Google Scholar]
  20. Cramer J. H., Sinsheimer R. L. Replication of bacteriophage MS2. X. Phage-specific ribonucleoprotein particles found in MS2-infected Escherichia coli. J Mol Biol. 1971 Nov 28;62(1):189–214. doi: 10.1016/0022-2836(71)90139-2. [DOI] [PubMed] [Google Scholar]
  21. Danziger R. E., Paranchych W. Stages in phage R17 infection. 3. Energy requirements for the F-pili mediated eclipse of viral infectivity. Virology. 1970 Mar;40(3):554–564. doi: 10.1016/0042-6822(70)90199-6. [DOI] [PubMed] [Google Scholar]
  22. Dube S. K., Rudland P. S. Control of translation by T4 phage: altered binding of disfavoured messengers. Nature. 1970 May 30;226(5248):820–823. doi: 10.1038/226820a0. [DOI] [PubMed] [Google Scholar]
  23. ELLIS D. B., PARANCHYCH W. SYNTHESIS OF RIBONUCLEIC ACID AND PROTEIN IN BACTERIA INFECTED WITH AN RNA BACTERIOPHAGE. J Cell Physiol. 1963 Oct;62:207–213. doi: 10.1002/jcp.1030620209. [DOI] [PubMed] [Google Scholar]
  24. Eggen K., Nathans D. Regulation of protein synthesis directed by coliphage MS2 RNA. II. In vitro repression by phage coat protein. J Mol Biol. 1969 Jan;39(2):293–305. doi: 10.1016/0022-2836(69)90318-0. [DOI] [PubMed] [Google Scholar]
  25. Eggen K., Oeschger M. P., Nathans D. Cell-free protein synthesis directed by colphage MS2 RNA: sequential synthesis of specific phage proteins. Biochem Biophys Res Commun. 1967 Aug 23;28(4):587–597. doi: 10.1016/0006-291x(67)90354-3. [DOI] [PubMed] [Google Scholar]
  26. Engelberg H., Soudry E. Inhibition of ribonucleic acid bacteriophage release from its host by rifampin. J Virol. 1971 Jun;7(6):847–848. doi: 10.1128/jvi.7.6.847-848.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Engelberg H., Soudry E. Ribonucleic acid bacteriophage release: requirement for host-controlled protein synthesis. J Virol. 1971 Sep;8(3):257–264. doi: 10.1128/jvi.8.3.257-264.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Engelhardt D. L., Robertson H. D., Zinder N. D. In vitro translation of multistranded RNA from Escherichia coli infected by bacteriophage f-2. Proc Natl Acad Sci U S A. 1968 Mar;59(3):972–979. doi: 10.1073/pnas.59.3.972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Engelhardt D. L., Webster R. E., Zinder N. D. Amber mutants and polarity in vitro. J Mol Biol. 1967 Oct 14;29(1):45–58. doi: 10.1016/0022-2836(67)90180-5. [DOI] [PubMed] [Google Scholar]
  30. Enger M. D., Kaesberg P. Comparative studies of the coat proteins of R-17 and M-12 bacteriophages. J Mol Biol. 1965 Aug;13(1):260–268. doi: 10.1016/s0022-2836(65)80095-x. [DOI] [PubMed] [Google Scholar]
  31. Fiers W., Contreras R., De Wachter R., Haegeman G., Merregaert J., Jou W. M., Vandenberghe A. Recent progress in the sequence determination of bacteriophage MS2 RNA. Biochimie. 1971;53(4):495–506. doi: 10.1016/s0300-9084(71)80167-0. [DOI] [PubMed] [Google Scholar]
  32. Fiers W., Van Montagu M., De Wachter R., Haegeman G., Min Jou W., Messens E., Remaut E., Vandenberghe A., Van Styvendaele B. Studies on the primary structure and the replication mechanism of bacteriophage RNA. Cold Spring Harb Symp Quant Biol. 1969;34:697–705. doi: 10.1101/sqb.1969.034.01.079. [DOI] [PubMed] [Google Scholar]
  33. Fromageot H. P., Zinder N. D. Growth of bacteriophage f2 in E. coli treated with rifampicin. Proc Natl Acad Sci U S A. 1968 Sep;61(1):184–191. doi: 10.1073/pnas.61.1.184. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Fukami H., Imahori K. Control of translation by the conformation of messenger RNA. Proc Natl Acad Sci U S A. 1971 Mar;68(3):570–573. doi: 10.1073/pnas.68.3.570. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. GESTELAND R. F., BOEDTKER H. SOME PHYSICAL PROPERTIES OF BACTERIOPHAGE R17 AND ITS RIBONUCLEIC ACID. J Mol Biol. 1964 Apr;8:496–507. doi: 10.1016/s0022-2836(64)80007-3. [DOI] [PubMed] [Google Scholar]
  36. Garwes D., Sillero A., Ochoa S. Virus-specific proteins in Escherichia coli infected with phage Qb. Biochim Biophys Acta. 1969 Jul 22;186(1):166–172. doi: 10.1016/0005-2787(69)90499-7. [DOI] [PubMed] [Google Scholar]
  37. Gesteland R. F., Spahr P. F. Translation of R-17 RNA fragments. Cold Spring Harb Symp Quant Biol. 1969;34:707–716. doi: 10.1101/sqb.1969.034.01.080. [DOI] [PubMed] [Google Scholar]
  38. Godson G. N., Sinsheimer R. L. The replication of bacteriophage MS2. VI. Interaction between bacteriophage RNA and cellular components in MS2-infected Escherichia coli. J Mol Biol. 1967 Feb 14;23(3):495–521. doi: 10.1016/s0022-2836(67)80121-9. [DOI] [PubMed] [Google Scholar]
  39. Godson G. N. Site of synthesis of viral ribonucleic acid and phage assembly in MS2-infected Escherichia coli. J Mol Biol. 1968 May 28;34(1):149–163. doi: 10.1016/0022-2836(68)90241-6. [DOI] [PubMed] [Google Scholar]
  40. Goodman H. M., Billeter M. A., Hindley J., Weissmann C. The nucleotide sequence at the 5'-terminus of the Q RNA minus trand. Proc Natl Acad Sci U S A. 1970 Oct;67(2):921–928. doi: 10.1073/pnas.67.2.921. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Granboulan N., Franklin R. M. High resolution autoradiography of Escherichia coli cells infected with bacteriophage R17. J Bacteriol. 1966 Feb;91(2):849–857. doi: 10.1128/jb.91.2.849-857.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Grubman M. J., Nakada D. Ribosomal subunits and MS2 phage RNA-directed protein synthesis. Nature. 1969 Sep 20;223(5212):1242–1247. doi: 10.1038/2231242a0. [DOI] [PubMed] [Google Scholar]
  43. Gupta S. L., Chen J., Schaefer L., Lengyel P., Weissman S. M. Nucleotide sequence of a ribosome attachment site of bacteriophage f2 RNA. Biochem Biophys Res Commun. 1970 Jun 5;39(5):883–888. doi: 10.1016/0006-291x(70)90406-7. [DOI] [PubMed] [Google Scholar]
  44. Gupta S. L., Waterson J., Sopori M. L., Weissman S. M., Lengyel P. Movement of the ribosome along the messenger ribonucleic acid during protein synthesis. Biochemistry. 1971 Nov 23;10(24):4410–4421. doi: 10.1021/bi00800a010. [DOI] [PubMed] [Google Scholar]
  45. Guthrie C., Nomura M. Initiation of protein synthesis: a critical test of the 30S subunit model. Nature. 1968 Jul 20;219(5151):232–235. doi: 10.1038/219232a0. [DOI] [PubMed] [Google Scholar]
  46. Haegeman G., Jou W. M., Fiers W. Studies on the bacteriophage MS2. IX. The heptanucleotide sequences present in the pancreatic ribonuclease digest of the viral RNA. J Mol Biol. 1971 May 14;57(3):597–613. doi: 10.1016/0022-2836(71)90112-4. [DOI] [PubMed] [Google Scholar]
  47. Haruna I., Spiegelman S. Specific template requirments of RNA replicases. Proc Natl Acad Sci U S A. 1965 Aug;54(2):579–587. doi: 10.1073/pnas.54.2.579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Haywood A. M., Harris J. M. Actinomycin inhibition of MS2 replication. J Mol Biol. 1966 Jul;18(3):448–463. doi: 10.1016/s0022-2836(66)80036-0. [DOI] [PubMed] [Google Scholar]
  49. Haywood A. M., Sinsheimer R. L. The replication of bacteriophage MS2. V. Proteins specifically associated with infection. J Mol Biol. 1965 Dec;14(2):305–326. doi: 10.1016/s0022-2836(65)80184-x. [DOI] [PubMed] [Google Scholar]
  50. Heisenberg M. Formation of defective bacteriophage particles by fr amber mutants. J Mol Biol. 1966 May;17(1):136–144. doi: 10.1016/s0022-2836(66)80100-6. [DOI] [PubMed] [Google Scholar]
  51. Helser T. L., Davies J. E., Dahlberg J. E. Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli. Nat New Biol. 1971 Sep 1;233(35):12–14. doi: 10.1038/newbio233012a0. [DOI] [PubMed] [Google Scholar]
  52. Hindley J., Staples D. H., Billeter M. A., Weissmann C. Location of the coat cistron on the RNA of phage Q-beta. Proc Natl Acad Sci U S A. 1970 Nov;67(3):1180–1187. doi: 10.1073/pnas.67.3.1180. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Hindley J., Staples D. H. Sequence of a ribosome binding site in bacteriophage Q-beta-RNA. Nature. 1969 Dec 6;224(5223):964–967. doi: 10.1038/224964a0. [DOI] [PubMed] [Google Scholar]
  54. Hohn T., Hohn B. Structure and assembly of simple RNA bacteriophages. Adv Virus Res. 1970;16:43–98. doi: 10.1016/s0065-3527(08)60021-4. [DOI] [PubMed] [Google Scholar]
  55. Hohn T. Studies on a possible precursor in the self assembly of the bacteriophage fr. Eur J Biochem. 1969 Apr;8(4):552–556. doi: 10.1111/j.1432-1033.1969.tb00562.x. [DOI] [PubMed] [Google Scholar]
  56. Horiuchi K., Matsuhashi S. Three cistrons in bacteriophage Q beta. Virology. 1970 Sep;42(1):49–60. doi: 10.1016/0042-6822(70)90237-0. [DOI] [PubMed] [Google Scholar]
  57. Horiuchi K., Webster R. E., Matsuhashi S. Gene products of bacteriophage Q beta. Virology. 1971 Aug;45(2):429–439. doi: 10.1016/0042-6822(71)90343-6. [DOI] [PubMed] [Google Scholar]
  58. Hotham-Iglewski B., Phillips L. A., Franklin R. M. Viral RNA transcription--translation complex in Escherichia coli infected with bacteriophage R17. Nature. 1968 Aug 17;219(5155):700–703. doi: 10.1038/219700a0. [DOI] [PubMed] [Google Scholar]
  59. Hsu W. T. Translation of an RNA viral message in vitro: one-step polypeptide chain elongation. Biochem Biophys Res Commun. 1971 Feb 5;42(3):405–412. doi: 10.1016/0006-291x(71)90385-8. [DOI] [PubMed] [Google Scholar]
  60. Hudson J. B., Paranchych W. Effect of bacteriophage R17 infection on host-directed synthesis of ribosomal ribonucleates. J Virol. 1967 Jun;1(3):529–537. doi: 10.1128/jvi.1.3.529-537.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Hung P. P., Ling C. M., Overby L. R. Self-assembly of Q-beta and MS2 phage particles: possible function of initiation complexes. Science. 1969 Dec 26;166(3913):1638–1640. doi: 10.1126/science.166.3913.1638. [DOI] [PubMed] [Google Scholar]
  62. Hung P. P., Overby L. R. Alteration in function of transfer ribonucleic acid of Escherichia coli after infection with phage Q beta. J Biol Chem. 1968 Nov 10;243(21):5525–5531. [PubMed] [Google Scholar]
  63. Hung P. P., Overby L. R. The reconstitution of infective bacteriophage Q beta. Biochemistry. 1969 Mar;8(3):820–828. doi: 10.1021/bi00831a009. [DOI] [PubMed] [Google Scholar]
  64. Hunt D., Saito Y., Watanabe M. Membrane-bound ribonucleic acid synthesis in Escherichia coli infected with ribonucleic acid bacteriophage R23. J Biol Chem. 1971 Jul 10;246(13):4151–4156. [PubMed] [Google Scholar]
  65. Hunt D., Watanabe M. The ribosomal-RNA synthesis factor psi-r in Escherichia coli infected with RNA bacteriophage R23. Biochem Biophys Res Commun. 1971 Nov;45(4):972–979. doi: 10.1016/0006-291x(71)90432-3. [DOI] [PubMed] [Google Scholar]
  66. Iglewski W. J., Franklin R. M., Schwartz J. H. The lack of messenger activity of ribonucleic acid complementary to the viral ribonucleic acid of bacteriophage R17. J Biol Chem. 1969 Feb 25;244(4):736–743. [PubMed] [Google Scholar]
  67. Iwasaki K., Sabol S., Wahba A. J., Ochoa S. Translation of the genetic message. VII. Role of initiation factors in formation of the chain initiation complex with Escherichia coli ribosomes. Arch Biochem Biophys. 1968 May;125(2):542–547. doi: 10.1016/0003-9861(68)90612-7. [DOI] [PubMed] [Google Scholar]
  68. Jacobson M. F., Asso J., Baltimore D. Further evidence on the formation of poliovirus proteins. J Mol Biol. 1970 May 14;49(3):657–669. doi: 10.1016/0022-2836(70)90289-5. [DOI] [PubMed] [Google Scholar]
  69. Jeppesen P. G., Steitz J. A., Gesteland R. F., Spahr P. F. Gene order in the bacteriophage R17 RNA: 5'-a protein-coat protein-synthetase-3'. Nature. 1970 Apr 18;226(5242):230–237. doi: 10.1038/226230a0. [DOI] [PubMed] [Google Scholar]
  70. Jockusch H., Ball L. A., Kaesberg P. Synthesis of polypeptides directed by the RNA of phage Q beta. Virology. 1970 Oct;42(2):401–414. doi: 10.1016/0042-6822(70)90283-7. [DOI] [PubMed] [Google Scholar]
  71. Kaerner H. C. Sequential steps in the in vivo assembly of the RNA bacteriophage fr. J Mol Biol. 1970 Nov 14;53(3):515–529. doi: 10.1016/0022-2836(70)90081-1. [DOI] [PubMed] [Google Scholar]
  72. Kamen R. Characterization of the subunits of Q-beta replicase. Nature. 1970 Nov 7;228(5271):527–533. doi: 10.1038/228527a0. [DOI] [PubMed] [Google Scholar]
  73. Kelly R. B., Sinsheimer R. L. The replication of bacteriophage MS2. VII. Non-conservative replication of double-stranded RNA. J Mol Biol. 1967 Jun 14;26(2):169–179. doi: 10.1016/0022-2836(67)90289-6. [DOI] [PubMed] [Google Scholar]
  74. Klem E. B., Hsu W. T., Weiss S. B. The selective inhibition of protein initiation by T4 phage-induced factors. Proc Natl Acad Sci U S A. 1970 Oct;67(2):696–701. doi: 10.1073/pnas.67.2.696. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Knolle P., Hohn T. R17 coat protein interaction with multi-stranded R17 RNA. Eur J Biochem. 1970 Sep;16(1):19–24. doi: 10.1111/j.1432-1033.1970.tb01048.x. [DOI] [PubMed] [Google Scholar]
  76. Kolakofsky D., Weissmann C. Possible mechanism for transition of viral RNA from polysome to replication complex. Nat New Biol. 1971 May 12;231(19):42–46. doi: 10.1038/newbio231042a0. [DOI] [PubMed] [Google Scholar]
  77. Kolakofsky D., Weissmann C. Q replicase as repressor of Q RNA-directed protein synthesis. Biochim Biophys Acta. 1971 Sep 24;246(3):596–599. doi: 10.1016/0005-2787(71)90799-4. [DOI] [PubMed] [Google Scholar]
  78. Kondo M., Eggerston G., Eisenstadt J., Lengyel P. Ribosome formation from subunits: dependence on formylmethionyl-transfer RNA in extracts from E. coli. Nature. 1968 Oct 26;220(5165):368–371. doi: 10.1038/220368a0. [DOI] [PubMed] [Google Scholar]
  79. Kondo M., Gallerani R., Weissmann C. Subunit structure of Q-beta replicase. Nature. 1970 Nov 7;228(5271):525–527. doi: 10.1038/228525a0. [DOI] [PubMed] [Google Scholar]
  80. Konigsberg W., Maita T., Katze J., Weber K. Amino-acid sequence of the "Qbeta" coat protein. Nature. 1970 Jul 18;227(5255):271–273. doi: 10.1038/227271a0. [DOI] [PubMed] [Google Scholar]
  81. Konings R. N., Ward R., Francke B., Hofschneider P. H. Gene order of RNA bacteriophage M 12. Nature. 1970 May 16;226(5246):604–607. doi: 10.1038/226604a0. [DOI] [PubMed] [Google Scholar]
  82. Kozak M., Nathans D. Fate of maturation protein during infection by coliphage MS2. Nat New Biol. 1971 Sep 15;234(50):209–211. doi: 10.1038/newbio234209a0. [DOI] [PubMed] [Google Scholar]
  83. Krueger R. G. Serological relatedness of the ribonucleic acid-containing coliphages. J Virol. 1969 Nov;4(5):567–573. doi: 10.1128/jvi.4.5.567-573.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Kuechler E., Rich A. Position of the initiator and peptidyl sites in the E. coli ribosome. Nature. 1970 Mar 7;225(5236):920–924. doi: 10.1038/225920a0. [DOI] [PubMed] [Google Scholar]
  85. Kuwano M., Schlessinger D., Morse D. E. Loss of dispensable endonuclease activity in relief of polarity by suA. Nat New Biol. 1971 Jun 16;231(24):214–217. doi: 10.1038/newbio231214a0. [DOI] [PubMed] [Google Scholar]
  86. LODISH H. F., COOPER S., ZINDER N. D. HOST-DEPENDENT MUTANTS OF THE BACTERIOPHAGE F2. IV. ON THE BIOSYNTHESIS OF A VIRAL RNA POLYMERASE. Virology. 1964 Sep;24:60–70. doi: 10.1016/0042-6822(64)90148-5. [DOI] [PubMed] [Google Scholar]
  87. LOEB T., ZINDER N. D. A bacteriophage containing RNA. Proc Natl Acad Sci U S A. 1961 Mar 15;47:282–289. doi: 10.1073/pnas.47.3.282. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Lee-Huang S., Ochoa S. Messenger discriminating species of initiation factor F3. Nat New Biol. 1971 Dec 22;234(51):236–239. doi: 10.1038/newbio234236a0. [DOI] [PubMed] [Google Scholar]
  89. Ling V. Sequence at the 5'-end of bacteriophage f2 RNA. Biochem Biophys Res Commun. 1971 Jan 8;42(1):82–88. doi: 10.1016/0006-291x(71)90365-2. [DOI] [PubMed] [Google Scholar]
  90. Lodish H. F. Bacteriophage f2 RNA: control of translation and gene order. Nature. 1968 Oct 26;220(5165):345–350. doi: 10.1038/220345a0. [DOI] [PubMed] [Google Scholar]
  91. Lodish H. F., Horiuchi K., Zinder N. D. Mutants of the bacteriophage f2. V. On the production of noninfectious phage particles. Virology. 1965 Oct;27(2):139–155. doi: 10.1016/0042-6822(65)90154-6. [DOI] [PubMed] [Google Scholar]
  92. Lodish H. F. Independent initiation of translation of two bacteriophage f2 proteins. Biochem Biophys Res Commun. 1969 Sep 24;37(1):127–136. doi: 10.1016/0006-291x(69)90890-0. [DOI] [PubMed] [Google Scholar]
  93. Lodish H. F. Independent translation of the genes of bacteriophage f2 RNA. J Mol Biol. 1968 Mar 28;32(3):681–685. doi: 10.1016/0022-2836(68)90351-3. [DOI] [PubMed] [Google Scholar]
  94. Lodish H. F. Polar effects of an amber mutation in f2 bacteriophage. J Mol Biol. 1968 Feb 28;32(1):47–58. doi: 10.1016/0022-2836(68)90144-7. [DOI] [PubMed] [Google Scholar]
  95. Lodish H. F., Robertson H. D. Cell-free synthesis of bacteriophage f2 maturation protein. J Mol Biol. 1969 Oct 14;45(1):9–22. doi: 10.1016/0022-2836(69)90206-x. [DOI] [PubMed] [Google Scholar]
  96. Lodish H. F., Robertson H. D. Regulation of in vitro translation of bacteriophage f2 RNA. Cold Spring Harb Symp Quant Biol. 1969;34:655–673. doi: 10.1101/sqb.1969.034.01.076. [DOI] [PubMed] [Google Scholar]
  97. Lodish H. F. Secondary structure of bacteriophage f2 ribonucleic acid and the initiation of in vitro protein biosynthesis. J Mol Biol. 1970 Jun 28;50(3):689–702. doi: 10.1016/0022-2836(70)90093-8. [DOI] [PubMed] [Google Scholar]
  98. Lodish H. F. Species specificity of polypeptide chain initiation. Nature. 1969 Nov 29;224(5222):867–870. doi: 10.1038/224867a0. [DOI] [PubMed] [Google Scholar]
  99. Lodish H. F. Specificity in bacterial protein synthesis: role of initiation factors and ribosomal subunits. Nature. 1970 May 23;226(5247):705–707. doi: 10.1038/226705a0. [DOI] [PubMed] [Google Scholar]
  100. Lodish H. F. The replication of RNA-containing bacteriophages. Prog Biophys Mol Biol. 1968;18:285–312. doi: 10.1016/0079-6107(68)90027-8. [DOI] [PubMed] [Google Scholar]
  101. Lodish H. F. Thermal melting of bacteriophage f2 RNA and initiation of synthesis of the maturation protein. J Mol Biol. 1971 Mar 28;56(3):627–632. doi: 10.1016/0022-2836(71)90406-2. [DOI] [PubMed] [Google Scholar]
  102. Lodish H. F., Zinder N. D. Mutants of the bacteriophage f2. 8. Control mechanisms for phage-specific syntheses. J Mol Biol. 1966 Aug;19(2):333–348. doi: 10.1016/s0022-2836(66)80008-6. [DOI] [PubMed] [Google Scholar]
  103. Lunt M. R., Sinsheimer R. L. Inhibition of ribonucleic acid bacteriophage growth by actinomycin D. J Mol Biol. 1966 Jul;18(3):541–546. doi: 10.1016/s0022-2836(66)80042-6. [DOI] [PubMed] [Google Scholar]
  104. Mitra S., Enger M. D., Kaesberg P. PHYSICAL AND CHEMICAL PROPERTIES OF RNA FROM THE BACTERIAL VIRUS R17. Proc Natl Acad Sci U S A. 1963 Jul;50(1):68–75. doi: 10.1073/pnas.50.1.68. [DOI] [PMC free article] [PubMed] [Google Scholar]
  105. Miyake T., Haruna I., Shiba T., Ito Y. H., Yamane K. Grouping of RNA phages based on the template specificity of their RNA replicases. Proc Natl Acad Sci U S A. 1971 Sep;68(9):2022–2024. doi: 10.1073/pnas.68.9.2022. [DOI] [PMC free article] [PubMed] [Google Scholar]
  106. Model P., Webster R. E., Zinder N. D. The UGA codon in vitro: chain termination and suppression. J Mol Biol. 1969 Jul 14;43(1):177–190. doi: 10.1016/0022-2836(69)90087-4. [DOI] [PubMed] [Google Scholar]
  107. Moore C. H., Farron F., Bohnert D., Weissmann C. Possible origin of a minor virus specific protein (A1) in Q-beta particles. Nat New Biol. 1971 Sep 15;234(50):204–206. doi: 10.1038/newbio234204a0. [DOI] [PubMed] [Google Scholar]
  108. Morse D. E., Guertin M. Regulation of mRNA utilization and degradation by amino-acid starvation. Nat New Biol. 1971 Aug 11;232(2):165–169. doi: 10.1038/newbio232165a0. [DOI] [PubMed] [Google Scholar]
  109. Morse D. E., Yanofsky C. Polarity and the degradation of mRNA. Nature. 1969 Oct 25;224(5217):329–331. doi: 10.1038/224329a0. [DOI] [PubMed] [Google Scholar]
  110. NATHANS D., NOTANI G., SCHWARTZ J. H., ZINDER N. D. Biosynthesis of the coat protein of coliphage f2 by E. coli extracts. Proc Natl Acad Sci U S A. 1962 Aug;48:1424–1431. doi: 10.1073/pnas.48.8.1424. [DOI] [PMC free article] [PubMed] [Google Scholar]
  111. Nathans D. Cell-free protein synthesis directed by coliphage MS2 RNA: synthesis of intact viral coat protein and other products. J Mol Biol. 1965 Sep;13(2):521–531. doi: 10.1016/s0022-2836(65)80114-0. [DOI] [PubMed] [Google Scholar]
  112. Nathans D., Oeschger M. P., Polmar S. K., Eggen K. Regulation of protein synthesis directed by coliphage MS2 RNA. I. Phage protein and RNA synthesis in cells infected with suppressible mutants. J Mol Biol. 1969 Jan;39(2):279–292. doi: 10.1016/0022-2836(69)90317-9. [DOI] [PubMed] [Google Scholar]
  113. Nichols J. L. Nucleotide sequence from the polypeptide chain termination region of the coat protein cistron in bacteriophage R17 RNA. Nature. 1970 Jan 10;225(5228):147–151. doi: 10.1038/225147a0. [DOI] [PubMed] [Google Scholar]
  114. Nichols J. L., Robertson H. D. Sequences of RNA fragments from the bacteriophage f2 coat protein cistron which differ from their R17 counterparts. Biochim Biophys Acta. 1971 Feb 11;228(3):676–681. doi: 10.1016/0005-2787(71)90731-3. [DOI] [PubMed] [Google Scholar]
  115. Nishihara T., Watanabe I. Discrete buoyant density distribution among RNA phages. Virology. 1969 Oct;39(2):360–362. doi: 10.1016/0042-6822(69)90063-4. [DOI] [PubMed] [Google Scholar]
  116. Nomura M., Lowry C. V., Guthrie C. The initiation of protein synthesis: joining of the 50S ribosomal subunit to the initiation complex. Proc Natl Acad Sci U S A. 1967 Oct;58(4):1487–1493. doi: 10.1073/pnas.58.4.1487. [DOI] [PMC free article] [PubMed] [Google Scholar]
  117. Nomura M., Lowry C. V. PHAGE f2 RNA-DIRECTED BINDING OF FORMYLMETHIONYL-TRNA TO RIBOSOMES AND THE ROLE OF 30S RIBOSOMAL SUBUNITS IN INITIATION OF PROTEIN SYNTHESIS. Proc Natl Acad Sci U S A. 1967 Sep;58(3):946–953. doi: 10.1073/pnas.58.3.946. [DOI] [PMC free article] [PubMed] [Google Scholar]
  118. OHTAKA Y., SPIEGELMAN S. TRANSLATIONAL CONTROL OF PROTEIN SYNTHESIS IN A CELL-FREE SYSTEM DIRECTED BY A POLYCISTRONIC VIRAL RNA. Science. 1963 Oct 25;142(3591):493–497. doi: 10.1126/science.142.3591.493. [DOI] [PubMed] [Google Scholar]
  119. Oeschger M. P., Nathans D. Differential synthesis of bacteriophage-specific proteins in MS2-infected Escherichia coli treated with actinomycin. J Mol Biol. 1966 Dec 28;22(2):235–247. doi: 10.1016/0022-2836(66)90129-x. [DOI] [PubMed] [Google Scholar]
  120. Osborn M., Weber K., Lodish H. F. Amino terminal peptides of RNA phage proteins synthesized in the cell free system. Biochem Biophys Res Commun. 1970 Nov 9;41(3):748–756. doi: 10.1016/0006-291x(70)90077-x. [DOI] [PubMed] [Google Scholar]
  121. Osborn M., Weiner A. M., Weber K. Large scale purification of A-protein from bacterior17. Eur J Biochem. 1970 Nov;17(1):63–67. doi: 10.1111/j.1432-1033.1970.tb01134.x. [DOI] [PubMed] [Google Scholar]
  122. Overby L. R., Barlow G. H., Doi R. H., Jacob M., Spiegelman S. Comparison of two serologically distinct ribonucleic acid bacteriophages. I. Properties of the viral particles. J Bacteriol. 1966 Jan;91(1):442–448. doi: 10.1128/jb.91.1.442-448.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  123. Overby L. R., Barlow G. H., Doi R. H., Jacob M., Spiegelman S. Comparison of two serologically distinct ribonucleic acid bacteriophages. II. Properties of the nucleic acids and coat proteins. J Bacteriol. 1966 Sep;92(3):739–745. doi: 10.1128/jb.92.3.739-745.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  124. Paranchych W., Krahn P. M., Bradley R. D. Stages in phage R17 infection. Virology. 1970 Jul;41(3):465–473. doi: 10.1016/0042-6822(70)90168-6. [DOI] [PubMed] [Google Scholar]
  125. Paranchych W. Stages in phage R17 infection: the role of divalent cations. Virology. 1966 Jan;28(1):90–99. doi: 10.1016/0042-6822(66)90309-6. [DOI] [PubMed] [Google Scholar]
  126. Passent J., Kaesberg P. Effect of rifampin on the development of ribonucleic acid bacteriophage Q . J Virol. 1971 Sep;8(3):286–292. doi: 10.1128/jvi.8.3.286-292.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  127. Pollack Y., Groner Y., Aviv(Greenshpan) H., Revel M. Role of initiation factor B (F3) in the preferential translation of T4 late messenger RNA in T4 infected E. Coli. FEBS Lett. 1970 Aug 17;9(4):218–221. doi: 10.1016/0014-5793(70)80359-3. [DOI] [PubMed] [Google Scholar]
  128. Revel M., Aviv(Greenshpan) H., Groner Y., Pollack Y. Fractionation of translation initiation factor B (F3) into cistron-specific species. FEBS Lett. 1970 Aug 17;9(4):213–217. doi: 10.1016/0014-5793(70)80358-1. [DOI] [PubMed] [Google Scholar]
  129. Revel M., Greenshpan H. Specificity in the binding of Escherichia coli ribosomes to natural messenger RNA. Eur J Biochem. 1970 Sep;16(1):117–122. doi: 10.1111/j.1432-1033.1970.tb01061.x. [DOI] [PubMed] [Google Scholar]
  130. Revel M., Herzberg M., Greenshpan H. Initiator protein dependent binding of messenger RNA to the ribosome. Cold Spring Harb Symp Quant Biol. 1969;34:261–275. doi: 10.1101/sqb.1969.034.01.032. [DOI] [PubMed] [Google Scholar]
  131. Richelson E., Nathans D. Association of bacteriophage proteins and RNA in E. coli infected with MS2. Biochem Biophys Res Commun. 1967 Dec 29;29(6):842–849. doi: 10.1016/0006-291x(67)90296-3. [DOI] [PubMed] [Google Scholar]
  132. Roberts J. W., Gussin G. N. Polarity in an amber mutant of bacteriophage R17. J Mol Biol. 1967 Dec 28;30(3):565–570. doi: 10.1016/0022-2836(67)90371-3. [DOI] [PubMed] [Google Scholar]
  133. Roberts J. W., Steitz J. E. The reconstitution of infective bacteriophage R17. Proc Natl Acad Sci U S A. 1967 Oct;58(4):1416–1421. doi: 10.1073/pnas.58.4.1416. [DOI] [PMC free article] [PubMed] [Google Scholar]
  134. Robertson H. D., Lodish H. F. Messenger characteristics of nascent bacteriophage RNA. Proc Natl Acad Sci U S A. 1970 Oct;67(2):710–716. doi: 10.1073/pnas.67.2.710. [DOI] [PMC free article] [PubMed] [Google Scholar]
  135. Robertson H., Webster R. E., Zinder N. D. Bacteriophage coat protein as repressor. Nature. 1968 May 11;218(5141):533–536. doi: 10.1038/218533a0. [DOI] [PubMed] [Google Scholar]
  136. Roufa D. J., Doctor B. P., Leder P. The two site model of ribosomal function: a test using degenerate serine codons in bacteriophage f2 mRNA. Biochem Biophys Res Commun. 1970 Apr 24;39(2):231–237. doi: 10.1016/0006-291x(70)90783-7. [DOI] [PubMed] [Google Scholar]
  137. Roufa D. J., Leder P. Biosynthesis of phage-specific initiation dipeptides. A purified biosynthetic system derived from Escherichia coli. J Biol Chem. 1971 May 25;246(10):3160–3167. [PubMed] [Google Scholar]
  138. Roufa D. J., Skogerson L. E., Leder P. Translation of phage Qbeta mRNA: a test of the two-site model for ribosomal function. Nature. 1970 Aug 8;227(5258):567–570. doi: 10.1038/227567a0. [DOI] [PubMed] [Google Scholar]
  139. Roumiantzeff M., Summers D. F., Maizel J. V., Jr In vitro protein synthetic activity of membrane-bound poliovirus polyribosomes. Virology. 1971 May;44(2):249–258. doi: 10.1016/0042-6822(71)90257-1. [DOI] [PubMed] [Google Scholar]
  140. SCOTT D. W. SEROLOGICAL CROSS REACTIONS AMONG THE RNA-CONTAINING COLIPHAGES. Virology. 1965 May;26:85–88. doi: 10.1016/0042-6822(65)90028-0. [DOI] [PubMed] [Google Scholar]
  141. SINHA N. K., FUJIMURA R. K., KAESBERG P. RIBONUCLEASE DIGESTION OF R17 VIRAL RNA. J Mol Biol. 1965 Jan;11:84–89. doi: 10.1016/s0022-2836(65)80173-5. [DOI] [PubMed] [Google Scholar]
  142. STRAUSS J. H., Jr, SINSHEIMER R. L. Purification and properties of bacteriophage MS2 and of its ribonucleic acid. J Mol Biol. 1963 Jul;7:43–54. doi: 10.1016/s0022-2836(63)80017-0. [DOI] [PubMed] [Google Scholar]
  143. Sabol S., Sillero M. A., Iwasaki K., Ochoa S. Purification and properties of initiation factor F3. Nature. 1970 Dec 26;228(5278):1269–1273. doi: 10.1038/2281269a0. [DOI] [PubMed] [Google Scholar]
  144. Schedl P. D., Singer R. E., Conway T. W. A factor required for the translation of bacteriophage f2 RNA in extracts of T4-infected cells. Biochem Biophys Res Commun. 1970 Feb 20;38(4):631–637. doi: 10.1016/0006-291x(70)90627-3. [DOI] [PubMed] [Google Scholar]
  145. Scolnick E., Tompkins R., Caskey T., Nirenberg M. Release factors differing in specificity for terminator codons. Proc Natl Acad Sci U S A. 1968 Oct;61(2):768–774. doi: 10.1073/pnas.61.2.768. [DOI] [PMC free article] [PubMed] [Google Scholar]
  146. Shapiro L., Franze de Fernandez M. T., August J. T. Resolution of two factors required in the Q-beta-RNA polymerase reaction. Nature. 1968 Nov 2;220(5166):478–480. doi: 10.1038/220478a0. [DOI] [PubMed] [Google Scholar]
  147. Shimura Y., Kaizer H., Nathans D. Fragments of MS2 RNA as messengers for specific bacteriophage proteins: fragments from fluorouracil-containing particles. J Mol Biol. 1968 Dec;38(3):453–455. doi: 10.1016/0022-2836(68)90402-6. [DOI] [PubMed] [Google Scholar]
  148. Skogerson L., Roufa D., Leder P. Characterization of the initial peptide of Q-beta RNA polymerase and control of its synthesis. Proc Natl Acad Sci U S A. 1971 Feb;68(2):276–279. doi: 10.1073/pnas.68.2.276. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Spahr P. F., Farber M., Gesteland R. F. Binding site on R17 RNA for coat protein. Nature. 1969 May 3;222(5192):455–458. doi: 10.1038/222455a0. [DOI] [PubMed] [Google Scholar]
  150. Spahr P. F., Gesteland R. F. Specific cleavage of bacteriophage R17 RNA by an endonuclease isolated from E. coli MRE-600. Proc Natl Acad Sci U S A. 1968 Mar;59(3):876–883. doi: 10.1073/pnas.59.3.876. [DOI] [PMC free article] [PubMed] [Google Scholar]
  151. Sparling P. F. Kasugamycin resistance: 30S ribosomal mutation with an unusual location on the Escherichia coli chromosome. Science. 1970 Jan 2;167(3914):56–58. doi: 10.1126/science.167.3914.56. [DOI] [PubMed] [Google Scholar]
  152. Staples D. H., Hindley J., Billeter M. A., Weissmann C. Localization of Q-beta maturation cistron ribosome binding site. Nat New Biol. 1971 Sep 15;234(50):202–204. doi: 10.1038/newbio234202a0. [DOI] [PubMed] [Google Scholar]
  153. Staples D. H., Hindley J. Ribosome binding site of Q-beta RNA polymerase cistron. Nat New Biol. 1971 Sep 15;234(50):211–212. doi: 10.1038/newbio234211a0. [DOI] [PubMed] [Google Scholar]
  154. Steitz J. A., Dube S. K., Rudland P. S. Control of translation of T4 phage: altered ribosome binding at R17 initiation sites. Nature. 1970 May 30;226(5248):824–827. doi: 10.1038/226824a0. [DOI] [PubMed] [Google Scholar]
  155. Steitz J. A. Identification of the A protein as a structural component of bacteriophage R17. J Mol Biol. 1968 May 14;33(3):923–936. doi: 10.1016/0022-2836(68)90328-8. [DOI] [PubMed] [Google Scholar]
  156. Steitz J. A. Isolation of the A protein from bacteriphage R17. J Mol Biol. 1968 May 14;33(3):937–945. doi: 10.1016/0022-2836(68)90329-x. [DOI] [PubMed] [Google Scholar]
  157. Steitz J. A. Polypeptide chain initiation: nucleotide sequences of the three ribosomal binding sites in bacteriophage R17 RNA. Nature. 1969 Dec 6;224(5223):957–964. doi: 10.1038/224957a0. [DOI] [PubMed] [Google Scholar]
  158. Stewart M. L., Grollman A. P., Huang M. T. Aurintricarboxylic acid: inhibitor of initiation of protein synthesis. Proc Natl Acad Sci U S A. 1971 Jan;68(1):97–101. doi: 10.1073/pnas.68.1.97. [DOI] [PMC free article] [PubMed] [Google Scholar]
  159. Strauss E. G., Kaesberg P. Acrylamide gel electrophoresis of bacteriophage Q beta: electrophoresis of the intact virions and of the viral proteins. Virology. 1970 Oct;42(2):437–452. doi: 10.1016/0042-6822(70)90287-4. [DOI] [PubMed] [Google Scholar]
  160. Strauss J. H., Jr, Sinsheimer R. L. Characterization of an infectivity assay for the ribonucleic acid of bacteriophage MS2. J Virol. 1967 Aug;1(4):711–716. doi: 10.1128/jvi.1.4.711-716.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  161. Strauss J. H., Jr, Sinsheimer R. L. Initial kinetics of degradation of MS2 ribonucleic acid by ribonuclease, heat and alkali and the presence of configurational restraints in this ribonucleic acid. J Mol Biol. 1968 Jun 28;34(3):453–465. doi: 10.1016/0022-2836(68)90172-1. [DOI] [PubMed] [Google Scholar]
  162. Sugiyama T., Hebert R. R., Hartman K. A. Ribonucleoprotein complexes formed between bacteriophage MS2 RNA and MS2 protein in vitro. J Mol Biol. 1967 May 14;25(3):455–463. doi: 10.1016/0022-2836(67)90198-2. [DOI] [PubMed] [Google Scholar]
  163. Sugiyama T., Nakada D. Control of translation of MS2 RNA cistrons by MS2 coat protein. Proc Natl Acad Sci U S A. 1967 Jun;57(6):1744–1750. doi: 10.1073/pnas.57.6.1744. [DOI] [PMC free article] [PubMed] [Google Scholar]
  164. Sugiyama T., Nakada D. Translational control of bacteriophage MS2 RNA cistrons by MS2 coat protein: affinity and specificity of the interaction of MS2 coat protein with MS2 RNA. J Mol Biol. 1970 Mar 14;48(2):349–355. doi: 10.1016/0022-2836(70)90166-x. [DOI] [PubMed] [Google Scholar]
  165. Sugiyama T., Nakada D. Translational control of bacteriophage MS2 RNA cistrons by MS2 coat protein: polyacrylamide gel electrophoretic analysis of proteins synthesized in vitro. J Mol Biol. 1968 Feb 14;31(3):431–440. doi: 10.1016/0022-2836(68)90419-1. [DOI] [PubMed] [Google Scholar]
  166. Sugiyama T., Stone H. O., Jr Protein synthesis directed by an amber coat-protein mutant of the RNA phage MS2. J Mol Biol. 1969 May 28;42(1):97–115. doi: 10.1016/0022-2836(69)90489-6. [DOI] [PubMed] [Google Scholar]
  167. Sugiyama T., Stone H. O., Jr Viral and bacterial protein syntheses in MS2-infected Escherichia coli cells. J Mol Biol. 1968 Aug 28;36(1):91–105. doi: 10.1016/0022-2836(68)90222-2. [DOI] [PubMed] [Google Scholar]
  168. Sugiyama T. Translational control of MS2 RNA cistrons. Cold Spring Harb Symp Quant Biol. 1969;34:687–694. doi: 10.1101/sqb.1969.034.01.078. [DOI] [PubMed] [Google Scholar]
  169. Swan D., Matthaei H. Further evidence for the four-site model of ribosomal function: Bacteriophage fr mRNA coded binding of AA-tRNA. FEBS Lett. 1971 Oct 1;17(2):215–220. doi: 10.1016/0014-5793(71)80150-3. [DOI] [PubMed] [Google Scholar]
  170. Takanami M., Yan Y., Jukes T. H. Studies on the site of ribosomal binding of f2 bacteriophage RNA. J Mol Biol. 1965 Jul;12(3):761–773. doi: 10.1016/s0022-2836(65)80325-4. [DOI] [PubMed] [Google Scholar]
  171. Thach S. S., Thach R. E. Translocation of messenger RNA and "accommodation" of fMet-tRNA. Proc Natl Acad Sci U S A. 1971 Aug;68(8):1791–1795. doi: 10.1073/pnas.68.8.1791. [DOI] [PMC free article] [PubMed] [Google Scholar]
  172. Thirion J. P., Kaesberg P. Base sequences of polypurine regions of the RNA's of bacteriophages R17 and M12. J Mol Biol. 1970 Jan 28;47(2):193–203. doi: 10.1016/0022-2836(70)90339-6. [DOI] [PubMed] [Google Scholar]
  173. Thirion J. P., Kaesberg P. The pyrimidine catalogs of M12 and R17 ribonucleic acids. J Mol Biol. 1968 Apr 28;33(2):379–393. doi: 10.1016/0022-2836(68)90196-4. [DOI] [PubMed] [Google Scholar]
  174. Tompkins R. K., Scolnick E. M., Caskey C. T. Peptide chain termination. VII. The ribosomal and release factor requirements for peptide release. Proc Natl Acad Sci U S A. 1970 Mar;65(3):702–708. doi: 10.1073/pnas.65.3.702. [DOI] [PMC free article] [PubMed] [Google Scholar]
  175. Tooze J., Weber K. Isolation and characterization of amber mutants of bacteriophage R17. J Mol Biol. 1967 Sep 14;28(2):311–330. doi: 10.1016/s0022-2836(67)80012-3. [DOI] [PubMed] [Google Scholar]
  176. Travers A. A., Kamen R. I., Schleif R. F. Factor necessary for ribosomal RNA synthesis. Nature. 1970 Nov 21;228(5273):748–751. doi: 10.1038/228748a0. [DOI] [PubMed] [Google Scholar]
  177. VALENTINE R. C., ENGELHARDT D. L., ZINDER N. D. HOST-DEPENDENT MUTANTS OF THE BACTERIOPHAGE F2. II. RESCUE AND COMPLEMENTATION OF MUTANTS. Virology. 1964 Jun;23:159–163. doi: 10.1016/0042-6822(64)90278-8. [DOI] [PubMed] [Google Scholar]
  178. VALENTINE R. C., STRAND M. COMPLEXES OF F-PILI AND RNA BACTERIOPHAGE. Science. 1965 Apr 23;148(3669):511–513. doi: 10.1126/science.148.3669.511. [DOI] [PubMed] [Google Scholar]
  179. Viñuela E., Algranati I. D., Feix G., Garwes D., Weissmann C., Ochoa S. Virus-specific proteins in Escherichia coli infected with some amber mutants of phage MS2. Biochim Biophys Acta. 1968 Feb 26;155(2):558–565. doi: 10.1016/0005-2787(68)90199-8. [DOI] [PubMed] [Google Scholar]
  180. Viñuela E., Algranati I. D., Ochoa S. Synthesis of virus-specific proteins in Escherichia coli infected with the RNA bacteriophage MS2. Eur J Biochem. 1967 Mar;1(1):3–11. doi: 10.1007/978-3-662-25813-2_2. [DOI] [PubMed] [Google Scholar]
  181. Viñuela E., Salas M., Ochoa S. Translation of the genetic message, iii. Formylmethionine as initiator of proteins programed by polycistronic messenger RNA. Proc Natl Acad Sci U S A. 1967 Mar;57(3):729–734. doi: 10.1073/pnas.57.3.729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  182. Vogel Z., Zamir A., Elson D. The possible involvement of peptidyl transferase in the termination step of protein biosynthesis. Biochemistry. 1969 Dec;8(12):5161–5168. doi: 10.1021/bi00840a070. [DOI] [PubMed] [Google Scholar]
  183. Voorma H. O., Benne R., Scholte ter Horst F. H. Binding of aminoacyl-tRNA to ribosomes programmed with bacteriophage MS2 RNA. J Mol Biol. 1969 Oct 28;45(2):423–428. doi: 10.1016/0022-2836(69)90116-8. [DOI] [PubMed] [Google Scholar]
  184. Voorma H. O., Benne R., den Hertog T. J. Binding of aminoacyl-tRNA to ribosomes programmed with bacteriophage MS2-RNA. Eur J Biochem. 1971 Feb;18(4):451–462. doi: 10.1111/j.1432-1033.1971.tb01263.x. [DOI] [PubMed] [Google Scholar]
  185. Voynow P., Kurland C. G. Stoichiometry of the 30S ribosomal proteins of Escherichia coli. Biochemistry. 1971 Feb 2;10(3):517–524. doi: 10.1021/bi00779a026. [DOI] [PubMed] [Google Scholar]
  186. Wahba A. J., Iwasaki K., Miller M. J., Sabol S., Sillero M. A., Vasquez C. Initiation of protein synthesis in Escherichia coli. II. Role of the initiation factors in polypeptide synthesis. Cold Spring Harb Symp Quant Biol. 1969;34:291–299. doi: 10.1101/sqb.1969.034.01.035. [DOI] [PubMed] [Google Scholar]
  187. Ward R., Konings R. N., Hofschneider P. H. Coat protein repression of bacteriophage M12 RNA directed polysome formation. Eur J Biochem. 1970 Nov;17(1):106–115. doi: 10.1111/j.1432-1033.1970.tb01142.x. [DOI] [PubMed] [Google Scholar]
  188. Ward R., Strans M., Valentine R. C. Translational repression of f2 protein synthesis. Biochem Biophys Res Commun. 1968 Feb 15;30(3):310–317. doi: 10.1016/0006-291x(68)90452-x. [DOI] [PubMed] [Google Scholar]
  189. Watanabe H., Watanabe M. Effect of infection with R23 on DNA and RNA synthesis in Escherichia coli. Can J Microbiol. 1971 Apr;17(4):461–466. doi: 10.1139/m71-077. [DOI] [PubMed] [Google Scholar]
  190. Watanabe M., Watanabe H., August J. T. Replication of RNA bacteriophage R23. I. Quantitative aspects of phage RNA and protein synthesis. J Mol Biol. 1968 Apr 14;33(1):1–20. doi: 10.1016/0022-2836(68)90277-5. [DOI] [PubMed] [Google Scholar]
  191. Weber K. Amino acid sequence studies on the tryptic peptides of the coat protein of the bacteriophage R17. Biochemistry. 1967 Oct;6(10):3144–3154. doi: 10.1021/bi00862a023. [DOI] [PubMed] [Google Scholar]
  192. Webster R. E., Engelhardt D. L., Zinder N. D. In vitro protein synthesis: chain initiation. Proc Natl Acad Sci U S A. 1966 Jan;55(1):155–161. doi: 10.1073/pnas.55.1.155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  193. Webster R. E., Engelhardt D. L., Zinder N. D., Konigsberg W. Amber mutants and chain termination in vitro. J Mol Biol. 1967 Oct 14;29(1):27–43. doi: 10.1016/0022-2836(67)90179-9. [DOI] [PubMed] [Google Scholar]
  194. Webster R. E., Robertson H. D., Zinder N. D. The 5'-terminus of f2 RNA and the coat protein gene. Cold Spring Harb Symp Quant Biol. 1969;34:675–685. doi: 10.1101/sqb.1969.034.01.077. [DOI] [PubMed] [Google Scholar]
  195. Webster R. E., Zinder N. D. Fate of the message-ribosome complex upon translation of termination signals. J Mol Biol. 1969 Jun 28;42(3):425–439. doi: 10.1016/0022-2836(69)90234-4. [DOI] [PubMed] [Google Scholar]
  196. Weiner A. M., Weber K. Natural read-through at the UGA termination signal of Q-beta coat protein cistron. Nat New Biol. 1971 Sep 15;234(50):206–209. doi: 10.1038/newbio234206a0. [DOI] [PubMed] [Google Scholar]
  197. Weissmann C., Ochoa S. Replication of phage RNA. Prog Nucleic Acid Res Mol Biol. 1967;6:353–399. doi: 10.1016/s0079-6603(08)60530-9. [DOI] [PubMed] [Google Scholar]
  198. Wittmann-Liebold B., Wittmann H. G. Coat proteins of strains of two RNA viruses: comparison of their amino acid sequences. Mol Gen Genet. 1967;100(4):358–363. doi: 10.1007/BF00334062. [DOI] [PubMed] [Google Scholar]
  199. ZINDER N. D., COOPER S. HOST-DEPENDENT MUTANTS OF THE BACTERIOPHAGE F2. I. ISOLATION AND PRELIMINARY CLASSIFICATION. Virology. 1964 Jun;23:152–158. doi: 10.1016/0042-6822(64)90277-6. [DOI] [PubMed] [Google Scholar]
  200. Zinder N. D., Engelhardt D. L., Webster R. E. Punctuation in the genetic code. Cold Spring Harb Symp Quant Biol. 1966;31:251–256. doi: 10.1101/sqb.1966.031.01.033. [DOI] [PubMed] [Google Scholar]
  201. de Wachter R., Merregaert J., Vandenberghe A., Contreras R., Fiers W. Studies on the bacteriophage MS2. The untranslated 5'-terminal nucleotide sequence preceding the first cistron. Eur J Biochem. 1971 Oct 14;22(3):400–414. doi: 10.1111/j.1432-1033.1971.tb01558.x. [DOI] [PubMed] [Google Scholar]

Articles from Bacteriological Reviews are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES