Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1979 Oct;140(1):125–130. doi: 10.1128/jb.140.1.125-130.1979

Isolation and characterization of mutations in the structural gene for protease III (ptr).

Y S Cheng, D Zipser, C Y Cheng, S J Rolseth
PMCID: PMC216787  PMID: 387716

Abstract

Escherichia coli mutants defective in protease III were isolated by enzyme assays of heavily mutagenized colones. One mutant produced thermolabile enzyme, and it is presumed to have a mutation in the structural gene of protease III. Two other mutants mapping at the same site had less than 5% of the wild-type protease III level. The genetic locus of these mutations, designated ptr, was located at approximately 60 min on the E. coli linkage map based on its high frequency (70%) of contransduction by P1 with argA. Strains with less than 5% of the wild-type protease III activity grew normally and degraded nonsense fragments of beta-galactosidase at wild-type rates.

Full text

PDF
125

Images in this article

127Image
on p.127

Selected References

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

  1. Bachmann B. J., Low K. B., Taylor A. L. Recalibrated linkage map of Escherichia coli K-12. Bacteriol Rev. 1976 Mar;40(1):116–167. doi: 10.1128/br.40.1.116-167.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bukhari A. I., Zipser D. Mutants of Escherichia coli with a defect in the degradation of nonsense fragments. Nat New Biol. 1973 Jun 20;243(129):238–241. doi: 10.1038/newbio243238a0. [DOI] [PubMed] [Google Scholar]
  3. Chang C. N., Blobel G., Model P. Detection of prokaryotic signal peptidase in an Escherichia coli membrane fraction: endoproteolytic cleavage of nascent f1 pre-coat protein. Proc Natl Acad Sci U S A. 1978 Jan;75(1):361–365. doi: 10.1073/pnas.75.1.361. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cheng Y. S., Zipser D. Purification and characterization of protease III from Escherichia coli. J Biol Chem. 1979 Jun 10;254(11):4698–4706. [PubMed] [Google Scholar]
  5. Goldberg A. L., St John A. C. Intracellular protein degradation in mammalian and bacterial cells: Part 2. Annu Rev Biochem. 1976;45:747–803. doi: 10.1146/annurev.bi.45.070176.003531. [DOI] [PubMed] [Google Scholar]
  6. Gottesman S., Zipser D. Deg phenotype of Escherichia coli lon mutants. J Bacteriol. 1978 Feb;133(2):844–851. doi: 10.1128/jb.133.2.844-851.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Inouye H., Beckwith J. Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitro. Proc Natl Acad Sci U S A. 1977 Apr;74(4):1440–1444. doi: 10.1073/pnas.74.4.1440. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Kowit J. D., Choy W. N., Champe S. P., Goldberg A. L. Role and location of "protease I" from Escherichia coli. J Bacteriol. 1976 Dec;128(3):776–784. doi: 10.1128/jb.128.3.776-784.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Miller C. G., Zipser D. Degradation of Escherichia coli beta-galactosidase fragments in protease-deficient mutants of Salmonella typhimurium. J Bacteriol. 1977 Apr;130(1):347–353. doi: 10.1128/jb.130.1.347-353.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Morrison S. L., Zipser D., Goldschmidt R. Polypeptide products of nonsense mutations. II. Minor fragments produced by nonsense mutations in the z gene of the lactose operon of Escherichia coli. J Mol Biol. 1971 Sep 28;60(3):485–497. doi: 10.1016/0022-2836(71)90183-5. [DOI] [PubMed] [Google Scholar]
  11. Morrison S. L., Zipser D. Polypeptide products of nonsense mutations. I. Termination fragments from nonsense mutations in the Z gene of the lac operon of Escherichia coli. J Mol Biol. 1970 Jun 14;50(2):359–371. doi: 10.1016/0022-2836(70)90198-1. [DOI] [PubMed] [Google Scholar]
  12. Norkin L. C. Marker-specific effects in genetic recombination. J Mol Biol. 1970 Aug;51(3):633–655. doi: 10.1016/0022-2836(70)90013-6. [DOI] [PubMed] [Google Scholar]
  13. Pacaud M., Richaud C. Protease II from Escherichia coli. Purification and characterization. J Biol Chem. 1975 Oct 10;250(19):7771–7779. [PubMed] [Google Scholar]
  14. Pacaud M., Uriel J. Isolation and some propeties of a proteolytic enzyme from Escherichia coli (protease I). Eur J Biochem. 1971 Dec 10;23(3):435–442. doi: 10.1111/j.1432-1033.1971.tb01638.x. [DOI] [PubMed] [Google Scholar]
  15. Regnier P., Thang M. N. Subcellular distribution and characterization of endo and exo-cellular proteases in E. coli. Biochimie. 1972;54(10):1227–1236. doi: 10.1016/s0300-9084(72)80063-4. [DOI] [PubMed] [Google Scholar]
  16. Roberts J. W., Roberts C. W., Craig N. L. Escherichia coli recA gene product inactivates phage lambda repressor. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4714–4718. doi: 10.1073/pnas.75.10.4714. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. WILLIAMS D. E., REISFELD R. A. DISC ELECTROPHORESIS IN POLYACRYLAMIDE GELS: EXTENSION TO NEW CONDITIONS OF PH AND BUFFER. Ann N Y Acad Sci. 1964 Dec 28;121:373–381. doi: 10.1111/j.1749-6632.1964.tb14210.x. [DOI] [PubMed] [Google Scholar]
  18. Zipser D., Zabell S., Rothman J., Grodzicker T., Wenk M. Fine structure of the gradient of polarity in the z gene of the lac operon of Escherichia coli. J Mol Biol. 1970 Apr 14;49(1):251–254. doi: 10.1016/0022-2836(70)90392-x. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES