Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1970 Oct;67(2):710–716. doi: 10.1073/pnas.67.2.710

Messenger Characteristics of Nascent Bacteriophage RNA*

Hugh D Robertson 1,2,†, Harvey F Lodish 1,2
PMCID: PMC283263  PMID: 5289017

Abstract

The proteins initiated in vitro by nascent bacteriophage f2 RNA strands attached to isolated replicating structures have been analyzed. The observations confirm that coat protein is the major product initiated and completed. Nascent strands direct the initiation of viral maturation protein in amounts similar to the maximum levels observed in vivo; this synthesis is independent of translation of the coat protein gene. However, only a fraction of these maturation protein molecules initiated in vitro is completed. Nascent RNA molecules also direct the initiation of appreciable amounts of viral RNA polymerase protein, very little of which is completed. Certain constraints on the in vitro translation of the polymerase gene from single-stranded RNA appear to be relaxed in the nascent strands, as indicated by the reduced effect of a polar amber mutation in the coat cistron upon polymerase protein initiation from nascent RNA.

Full text

PDF
710

Selected References

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

  1. 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]
  2. 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]
  3. Franklin R. M. Purification and properties of the replicative intermediate of the RNA bacteriophage R17. Proc Natl Acad Sci U S A. 1966 Jun;55(6):1504–1511. doi: 10.1073/pnas.55.6.1504. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. Morse D. E., Mosteller R., Baker R. F., Yanofsky C. Direction of in vivo degradation of tryptophan messenger RNA--a correction. Nature. 1969 Jul 5;223(5201):40–43. doi: 10.1038/223040a0. [DOI] [PubMed] [Google Scholar]
  14. 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]
  15. Robertson H. D., Webster R. E., Zinder N. D. Purification and properties of ribonuclease III from Escherichia coli. J Biol Chem. 1968 Jan 10;243(1):82–91. [PubMed] [Google Scholar]
  16. Robertson H. D., Zinder N. D. Identification of the terminus of nascent f2 bacteriophage RNA. Nature. 1968 Oct 5;220(5162):69–69. doi: 10.1038/220069a0. [DOI] [PubMed] [Google Scholar]
  17. Robertson H. D., Zinder N. D. Purification and properties of nascent f2 phage ribonucleic acid. J Biol Chem. 1969 Nov 10;244(21):5790–5800. [PubMed] [Google Scholar]
  18. 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]
  19. 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]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES