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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
. 1983 Apr;80(7):2059–2062. doi: 10.1073/pnas.80.7.2059

Stabilization of proteins by a bacteriophage T4 gene cloned in Escherichia coli.

L D Simon, B Randolph, N Irwin, G Binkowski
PMCID: PMC393752  PMID: 6340113

Abstract

The cloned bacteriophage T4 pin gene functions to stabilize several different kinds of proteins in Escherichia coli bacteria. Incomplete proteins such as puromycyl polypeptides, abnormal but complete proteins such as the lambda phage tsO protein, and labile eukaryotic proteins encoded by genes cloned in E. coli such as mature human fibroblast interferon are stabilized in cells in which the T4 pin gene is expressed. The cloned T4 pin gene does not seem to affect the turnover of normal E. coli proteins.

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Selected References

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

  1. Backman K., Ptashne M. Maximizing gene expression on a plasmid using recombination in vitro. Cell. 1978 Jan;13(1):65–71. doi: 10.1016/0092-8674(78)90138-1. [DOI] [PubMed] [Google Scholar]
  2. Bastia D., Germino J., Crosa J. H., Hale P. Molecular cloning of the replication terminus of the plasmid R6K. Gene. 1981 Jun-Jul;14(1-2):81–89. doi: 10.1016/0378-1119(81)90150-5. [DOI] [PubMed] [Google Scholar]
  3. Celis J. E., Smith J. D., Brenner S. Correlation between genetic and translational maps of gene 23 in bacteriophage T4. Nat New Biol. 1973 Jan 31;241(109):130–132. doi: 10.1038/newbio241130a0. [DOI] [PubMed] [Google Scholar]
  4. Charette M. F., Henderson G. W., Markovitz A. ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4728–4732. doi: 10.1073/pnas.78.8.4728. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gentz R., Langner A., Chang A. C., Cohen S. N., Bujard H. Cloning and analysis of strong promoters is made possible by the downstream placement of a RNA termination signal. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4936–4940. doi: 10.1073/pnas.78.8.4936. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. Goldschmidt R. In vivo degradation of nonsense fragments in E. coli. Nature. 1970 Dec 19;228(5277):1151–1154. doi: 10.1038/2281151a0. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Guarente L., Lauer G., Roberts T. M., Ptashne M. Improved methods for maximizing expression of a cloned gene: a bacterium that synthesizes rabbit beta-globin. Cell. 1980 Jun;20(2):543–553. doi: 10.1016/0092-8674(80)90640-6. [DOI] [PubMed] [Google Scholar]
  10. Guarente L., Roberts T. M., Ptashne M. A technique for expressing eukaryotic genes in bacteria. Science. 1980 Sep 19;209(4463):1428–1430. doi: 10.1126/science.6158095. [DOI] [PubMed] [Google Scholar]
  11. Itakura K., Hirose T., Crea R., Riggs A. D., Heyneker H. L., Bolivar F., Boyer H. W. Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin. Science. 1977 Dec 9;198(4321):1056–1063. doi: 10.1126/science.412251. [DOI] [PubMed] [Google Scholar]
  12. Lin S., Zabin I. Beta-galactosidase. Rates of synthesis and degradation of incomplete chains. J Biol Chem. 1972 Apr 10;247(7):2205–2211. [PubMed] [Google Scholar]
  13. Mount D. W. The genetics of protein degradation in bacteria. Annu Rev Genet. 1980;14:279–319. doi: 10.1146/annurev.ge.14.120180.001431. [DOI] [PubMed] [Google Scholar]
  14. Nagata S., Taira H., Hall A., Johnsrud L., Streuli M., Ecsödi J., Boll W., Cantell K., Weissmann C. Synthesis in E. coli of a polypeptide with human leukocyte interferon activity. Nature. 1980 Mar 27;284(5754):316–320. doi: 10.1038/284316a0. [DOI] [PubMed] [Google Scholar]
  15. Pine M. J. Steady-state measurement of the turnover of amino acid in the cellular proteins of growing Escherichia coli: existence of two kinetically distinct reactions. J Bacteriol. 1970 Jul;103(1):207–215. doi: 10.1128/jb.103.1.207-215.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Roberts T. M., Bikel I., Yocum R. R., Livingston D. M., Ptashne M. Synthesis of simian virus 40 t antigen in Escherichia coli. Proc Natl Acad Sci U S A. 1979 Nov;76(11):5596–5600. doi: 10.1073/pnas.76.11.5596. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Roberts T. M., Kacich R., Ptashne M. A general method for maximizing the expression of a cloned gene. Proc Natl Acad Sci U S A. 1979 Feb;76(2):760–764. doi: 10.1073/pnas.76.2.760. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Shineberg B., Zipser D. The ion gene and degradation of beta-galactosidase nonsense fragments. J Bacteriol. 1973 Dec;116(3):1469–1471. doi: 10.1128/jb.116.3.1469-1471.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Simon L. D., Tomczak K., St John A. C. Bacteriophages inhibit degradation of abnormal proteins in E. coli. Nature. 1978 Oct 5;275(5679):424–428. doi: 10.1038/275424a0. [DOI] [PubMed] [Google Scholar]
  20. Tacon W., Carey N., Emtage S. The construction and characterisation of plasmid vectors suitable for the expression of all DNA phases under the control of the E. coli tryptophan promoter. Mol Gen Genet. 1980 Feb;177(3):427–438. doi: 10.1007/BF00271481. [DOI] [PubMed] [Google Scholar]
  21. Taniguchi T., Guarente L., Roberts T. M., Kimelman D., Douhan J., 3rd, Ptashne M. Expression of the human fibroblast interferon gene in Escherichia coli. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5230–5233. doi: 10.1073/pnas.77.9.5230. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Yen C., Green L., Miller C. G. Degradation of intracellular protein in Salmonella typhimurium peptidase mutants. J Mol Biol. 1980 Oct 15;143(1):21–33. doi: 10.1016/0022-2836(80)90122-9. [DOI] [PubMed] [Google Scholar]

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