Abstract
Mutants of Salmonella typhimurium containing 1 to 2% of wild-type ribonuclease I activity were isolated. The rns mutation had no effect on the polarity of mutations in the S. typhimurium histidine operon. Even in the presence of an rns mutation, it was not possible to obtain strong suppressors of the polarity of two polar mutations in the his operon.
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Selected References
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- BECKWITH J. RESTORATION OF OPERON ACTIVITY BY SUPPRESSORS. Biochim Biophys Acta. 1963 Sep 17;76:162–164. [PubMed] [Google Scholar]
- Berkowitz D., Hushon J. M., Whitfield H. J., Jr, Roth J., Ames B. N. Procedure for identifying nonsense mutations. J Bacteriol. 1968 Jul;96(1):215–220. doi: 10.1128/jb.96.1.215-220.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bothwell A. L., Apirion D. Is RNase V a manifestation of RNase II? Biochem Biophys Res Commun. 1971 Aug 20;44(4):844–851. doi: 10.1016/0006-291x(71)90788-1. [DOI] [PubMed] [Google Scholar]
- 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]
- Chakraburtty K., Burma D. P. The purification and properties of a ribonuclease from Salmonella typhimurium extract. J Biol Chem. 1968 Mar 25;243(6):1133–1139. [PubMed] [Google Scholar]
- Contesse G., Naono S., Gros F. Effet des mutations polaires sur la transcription de l'opéron lactose chez Escherichia coli. C R Acad Sci Hebd Seances Acad Sci D. 1966 Oct 10;263(15):1007–1010. [PubMed] [Google Scholar]
- Corte G., Schlessinger D., Longo D., Venkov P. Transformation of 17 s to 16 s ribosomal RNA using ribonuclease II of Escherichia coli. J Mol Biol. 1971 Sep 14;60(2):325–338. doi: 10.1016/0022-2836(71)90297-x. [DOI] [PubMed] [Google Scholar]
- Dürwald H., Hoffmann-Berling H. Endonuclease-I-deficient and ribonuclease I-deficient Escherichia coli mutants. J Mol Biol. 1968 Jul 14;34(2):331–346. doi: 10.1016/0022-2836(68)90257-x. [DOI] [PubMed] [Google Scholar]
- ELSON D. Latent enzymic activity of a ribonucleoprotein isolated from Escherichia coli. Biochim Biophys Acta. 1959 Dec;36:372–386. doi: 10.1016/0006-3002(59)90179-9. [DOI] [PubMed] [Google Scholar]
- Fink G. R., Klopotowski T., Ames B. N. Histidine regulatory mutants in Salmonella typhimurium. IV. A positive selection for polar histidine-requiring mutants from histidine operator constitutive mutants. J Mol Biol. 1967 Nov 28;30(1):81–95. doi: 10.1016/0022-2836(67)90245-8. [DOI] [PubMed] [Google Scholar]
- Garen A. Sense and nonsense in the genetic code. Three exceptional triplets can serve as both chain-terminating signals and amino acid codons. Science. 1968 Apr 12;160(3824):149–159. doi: 10.1126/science.160.3824.149. [DOI] [PubMed] [Google Scholar]
- Gesteland R. F. Isolation and characterization of ribonuclease I mutants of Escherichia coli. J Mol Biol. 1966 Mar;16(1):67–84. doi: 10.1016/s0022-2836(66)80263-2. [DOI] [PubMed] [Google Scholar]
- Hilton J. L., Kearney P. C., Ames B. N. Mode of action of the herbicide, 3-amino-1,2,4-triazole(amitrole): inhibition of an enzyme of histidine biosynthesis. Arch Biochem Biophys. 1965 Dec;112(3):544–547. doi: 10.1016/0003-9861(65)90093-7. [DOI] [PubMed] [Google Scholar]
- Holmes R. K., Singer M. F. Inability to detect RNase V in Escherichia coli and comparison of other ribonucleases before and after infection with coliphage T7. Biochem Biophys Res Commun. 1971 Aug 20;44(4):837–843. doi: 10.1016/0006-291x(71)90787-x. [DOI] [PubMed] [Google Scholar]
- Imamoto F. Evidence for premature termination of transcription of the tryptophan operon in polarity mutants of Escherichia coli. Nature. 1970 Oct 17;228(5268):232–235. doi: 10.1038/228232a0. [DOI] [PubMed] [Google Scholar]
- Imamoto F., Kano Y. Inhibition of transcription of the tryptophan operon in Escherichia coli by a block in initiation of translation. Nat New Biol. 1971 Aug 11;232(2):169–173. doi: 10.1038/newbio232169a0. [DOI] [PubMed] [Google Scholar]
- Imamoto F., Yanofsky C. Transcription of the tryptophan operon in polarity mutants of Escherichia coli. II. Evidence for normal production of tryp-mRNA molecules and for premature termination of transcription. J Mol Biol. 1967 Aug 28;28(1):25–35. doi: 10.1016/s0022-2836(67)80074-3. [DOI] [PubMed] [Google Scholar]
- Kivity-Vogel T., Elson D. A correlation between ribonuclease II and the in vivo inactivation of messenger RNA in E. coli. Biochem Biophys Res Commun. 1968 Nov 8;33(3):412–417. doi: 10.1016/0006-291x(68)90587-1. [DOI] [PubMed] [Google Scholar]
- Kivity-Vogel T., Elson D. On the metabolic inactivation of messenger RNA in Escherichia coli: ribonuclease I and polynucleotide phosphorylase. Biochim Biophys Acta. 1967 Mar 29;138(1):66–75. doi: 10.1016/0005-2787(67)90586-2. [DOI] [PubMed] [Google Scholar]
- 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]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Martin R. G., Silbert D. F., Smith W. E., Whitfield H. J., Jr Polarity in the histidine operon. J Mol Biol. 1966 Nov 14;21(2):357–369. doi: 10.1016/0022-2836(66)90104-5. [DOI] [PubMed] [Google Scholar]
- Martin R. G., Whitfield H. J., Jr, Berkowitz D. B., Voll M. J. A molecular model of the phenomenon of polarity. Cold Spring Harb Symp Quant Biol. 1966;31:215–220. doi: 10.1101/sqb.1966.031.01.029. [DOI] [PubMed] [Google Scholar]
- 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]
- Morse D. E. Polarity induced by chloramphenicol and relief by suA. J Mol Biol. 1971 Jan 14;55(1):113–118. doi: 10.1016/0022-2836(71)90285-3. [DOI] [PubMed] [Google Scholar]
- Morse D. E., Primakoff P. Relief of polarity in E. coli by "suA". Nature. 1970 Apr 4;226(5240):28–31. doi: 10.1038/226028a0. [DOI] [PubMed] [Google Scholar]
- 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]
- Murray M. L., Hartman P. E. Overproduction of hisH and hisF gene products leads to inhibition of cell cell division in Salmonella. Can J Microbiol. 1972 May;18(5):671–681. doi: 10.1139/m72-105. [DOI] [PubMed] [Google Scholar]
- NEU H. C., HEPPEL L. A. THE RELEASE OF RIBONUCLEASE INTO THE MEDIUM WHEN ESCHERICHIA COLI CELLS ARE CONVERTED TO SPEROPLASTS. J Biol Chem. 1964 Nov;239:3893–3900. [PubMed] [Google Scholar]
- Ray R. K., Burma D. P. Partial purification and properties of a K plus-and minus and Mg2-plus or minus dependent phosphodiesterase from Salmonella typhimurium. Biochim Biophys Acta. 1970 Jul 15;212(1):102–110. doi: 10.1016/0005-2744(70)90182-8. [DOI] [PubMed] [Google Scholar]
- Rechler M. M., Bruni C. B., Martin R. G., Terry W. An intercistronic region in the histidine operon of Salmonella typhimurium. J Mol Biol. 1972 Aug 28;69(3):427–452. doi: 10.1016/0022-2836(72)90256-2. [DOI] [PubMed] [Google Scholar]
- Rechler M. M., Martin R. G. The intercistronic divide: translation of an intercistronic region in the histidine operon of Salmonella typhimurium. Nature. 1970 Jun 6;226(5249):908–911. doi: 10.1038/226908a0. [DOI] [PubMed] [Google Scholar]
- Reiner A. M. Genetic locus for ribonuclease I in Escherichia coli. J Bacteriol. 1969 Mar;97(3):1522–1523. doi: 10.1128/jb.97.3.1522-1523.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Riddle D. L., Roth J. R. Suppressors of frameshift mutations in Salmonella typhimurium. J Mol Biol. 1970 Nov 28;54(1):131–144. doi: 10.1016/0022-2836(70)90451-1. [DOI] [PubMed] [Google Scholar]
- 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]
- Roth J. R., Antón D. N., Hartman P. E. Histidine regulatory mutants in Salmonella typhimurium. I. Isolation and general properties. J Mol Biol. 1966 Dec 28;22(2):305–323. doi: 10.1016/0022-2836(66)90134-3. [DOI] [PubMed] [Google Scholar]
- Scaife J., Beckwith J. R. Mutational alteration of the maximal level of Lac operon expression. Cold Spring Harb Symp Quant Biol. 1966;31:403–408. doi: 10.1101/sqb.1966.031.01.052. [DOI] [PubMed] [Google Scholar]
- Singer M. F., Tolbert G. Purification and properties of a potassium-activated phosphodiesterase (RNAase II) from Escherichia coli. Biochemistry. 1965 Jul;4(7):1319–1330. doi: 10.1021/bi00883a016. [DOI] [PubMed] [Google Scholar]
- Smith H. O., Levine M. A phage P22 gene controlling integration of prophage. Virology. 1967 Feb;31(2):207–216. doi: 10.1016/0042-6822(67)90164-x. [DOI] [PubMed] [Google Scholar]
- 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]
- Summers W. C. Untranslated T7 phage mRNA is stabilized in suA host. Nat New Biol. 1971 Apr 14;230(15):208–208. doi: 10.1038/newbio230208a0. [DOI] [PubMed] [Google Scholar]
- VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
- 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]
- Whitfield H. J., Jr, Martin R. G., Ames B. N. Classification of aminotransferase (C gene) mutants in the histidine operon. J Mol Biol. 1966 Nov 14;21(2):335–355. doi: 10.1016/0022-2836(66)90103-3. [DOI] [PubMed] [Google Scholar]
- Yanofsky C., Ito J. Nonsense codons and polarity in the tryptophan operon. J Mol Biol. 1966 Nov 14;21(2):313–334. doi: 10.1016/0022-2836(66)90102-1. [DOI] [PubMed] [Google Scholar]
- Zipser D. Polar mutations and operon function. Nature. 1969 Jan 4;221(5175):21–25. doi: 10.1038/221021a0. [DOI] [PubMed] [Google Scholar]
