Skip to main content
Log in

Salmonella typhimurium mutations affecting utilization of L-leucine β-naphthylamide

  • Published:
Molecular and General Genetics MGG Aims and scope Submit manuscript

Summary

L-leucine-β-naphthylamide (LNA) will support growth of a leucine auxotroph of Salmonella typhimurium. Utilization of this compound depends on the presence in the cells of active peptidase N. Selection for improved growth on a suboptimal concentration of LNA yields mutants some of which contain elevated levels of peptidase N. The properties of these strains indicate that they carry tandem genetic duplications of the pepN locus: they show rec-dependent genetic instability; they contain an approximately doubled level of the pepN gene product; neighboring chromosomal loci are also duplicated; and, the mutants occur with a greatly diminished frequency in rec strains. When selection for improved growth on LNA is applied to a rec strain, the mutants obtained do not contain duplications. These strains appear to contain lesions in the pepN gene that lead to the production of a peptidase N with altered substrate specificity.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Anderson RP, Roth JR (1977) Tandem genetic duplications in phage and bacteria. Annu Rev Microbiol 31:473–505

    Google Scholar 

  • Anderson RP, Roth JR (1978a) Tandem genetic duplications in Salmonella typhimurium: amplification of the histidine operon. J Mol Biol 126:53–71

    Google Scholar 

  • Anderson RP, Roth JR (1978b) Gene duplication in bacteria: alteration of gene dosage by sister-chromosome exchanges. Cold Spring harbor Symp Quant Biol 43:1083–1087

    Google Scholar 

  • Behal FJ, Cox ST (1968) Arylamidase of Neisseria catarrhalis. J Bacteriol 96:1240–1248

    Google Scholar 

  • Lazdunski C, Busuttil J, Lazdunski A (1975a) Purification and properties of a periplasmic aminoendopeptidase from Escherichia coli. Eur J Biochem 60:363–369

    Google Scholar 

  • Lazdunski A, Murgier M, Lazdunski C (1975b) Evidence for an aminopeptidase localized near the cell surface of Escherichia coli: Regulation of synthesis by inorganic phosphate. Eur J Biochem 60:349–355

    Google Scholar 

  • Lazdunski A, Pellissier C, Lazdunski C (1975c) Regulation of Escherichia coli K10 aminoendopeptidase synthesis: Effects of mutations involved in the regulation of alkaline phosphatase. Eur J Biochem 60:357–362

    Google Scholar 

  • Lee HJ, LaRue JN, Wilson IB (1971) A simple spectrophotometric assay for aminoacyl arylamidases (naphthylamidases, aminopeptidases). Anal Biochem 41:397–401

    Google Scholar 

  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275

    Google Scholar 

  • Miller CG (1975) Genetic mapping of Salmonella typhimurium peptidase mutations. J Bacteriol 122:171–176

    Google Scholar 

  • Miller CG, MacKinnon K (1974) Peptidase mutants of Salmonella typhimurium. J Bacteriol 120:355–363

    Google Scholar 

  • Miller CG, Schwartz G (1978) Peptidase-deficient mutants of Escherichia coli. J Bacteriol 135:603–611

    Google Scholar 

  • Rigby PWJ, Burleigh BD Jr, Hartley BS (1974) Gene duplication in experimental enzyme evolution. Nature 251:200–204

    Google Scholar 

  • Roth JR (1970) Genetic techniques in studies of bacterial metabolism. In: Tabor H, Tabor CW (eds) Methods in enzymology, vol 17A. Academic Press, New York, pp 3–35

    Google Scholar 

  • Schmieger H (1972) Phage P 22 mutants with increased or decreased transduction abilities Mol Gen Gent 119:75–88

    Google Scholar 

  • Vogel HJ, Bonner DM (1956) Acetylornithinase of Escherichia coli: Partial purification and some properties. J Biol Chem 218:97–106

    Google Scholar 

  • Yan Y, Demerec M (1965) Genetic analysis of pyrimidine mutants of Salmonella typhimurium. Genetics 52:643–651

    Google Scholar 

  • Yang LM, Somerville RL (1976) Purification and properties of a new aminopeptidase from Escherichia coli K12. Biochim Biophys Acta 445:406–419

    Google Scholar 

  • Yen C, Green L, Miller CG (1980a) Degradation of intracellular protein in Salmonella typhimurium peptidase mutants. J Mol Biol 143:21–33

    Google Scholar 

  • Yen C, Green L, Miller CG (1980b) Peptide accumulation during growth of Salmonella typhimurium peptidase mutants. J Mol Biol 143:35–48

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

Communicated by G. O'Donovan

Rights and permissions

Reprints and permissions

About this article

Cite this article

Miller, C.G., Green, L. & Schultz, R. Salmonella typhimurium mutations affecting utilization of L-leucine β-naphthylamide. Mol Gen Genet 186, 228–234 (1982). https://doi.org/10.1007/BF00331854

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00331854

Keywords

Navigation