Protein degradation in E. coli: The ion mutation and bacteriophage lambda N and cll protein stability

Susan Gottesman, Max Gottesman, Jocelyn E. Shaw, Mark L. Pearson

Research output: Contribution to journalArticlepeer-review

135 Scopus citations

Abstract

The Ion gene of E. coli controls the stability of two bacteriophage lambda proteins. The functional half-life of the phage N gene product, measured by complementation, is increased about 5-fold in Ion mutant strains, from 2 min to 10 min. The chemical half-life of N protein, determined by its disappearance on polyacrylamide gels following pulse-chase labeling, increases about three-fold in Ion cells. In contrast to its effect on the N protein, the Ion mutation produces a 50% decrease in the chemical half-life of cll protein. The decay rate of many other phage proteins, including the unstable gene O product, remains unaffected by a host Ion defect. A Ion mutation alters lambda physiology in two ways. First, upon infection, the phage enters the lytic pathway predominantly. This may result from the deficiency of cll protein caused by its decreased stability, since cll product is required for establishment of lysogeny. Second, brief thermal induction of a Ion (λc1857) lysogen leads irreversibly to lysis; repression cannot be restablished and the treated cells are committed to forming infective centers. Although N product is normally required for rapid commitment, Ion lysogens become committed more rapidly than Ion+ lysogens, even in the absence of N function. These results identify for the first time native proteins whose stability is affected by the Lon proteolytic pathway. They also indicate that the Lon system may be important in regulating gene expression in E. coli.

Original languageEnglish (US)
Pages (from-to)225-233
Number of pages9
JournalCell
Volume24
Issue number1
DOIs
StatePublished - Apr 1981

Bibliographical note

Funding Information:
This work was supported in part by grants from the Medical Research Council of Canada, the National Institute for General Medical Sciences and the National Institutes of Health, and a contract to Litton Bionetics. Inc. from the National Cancer Institute. We would like to thank P. Trisler for excellent technical help. We would also like to thank Amos Oppenheim, Nancy Craig, Michael Yarmolinsky and Richard Roblin for their comments on the manuscript. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Copyright:
Copyright 2019 Elsevier B.V., All rights reserved.

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