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PMID: 146704 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Deg phenotype of Escherichia coli lon mutants.

Journal of bacteriology ·Vol. 133 ·No. 2 ·1978-02-00 ·Pages 844-51

Gottesman S, Zipser D

Abstract

Deg. one of the Escherichia coli systems for degrading abnormal polypeptides (e.g., nonsense fragments), is also involved in the degradation of some classes of missense proteins. Both missense proteins of beta-galactosidase and temperature-sensitive phage products appear to be degraded by the Deg system. Mutations in the Deg system are indistinguishable from mutations classically called lon or capR; all map near proC, all are mucoid, defective in protein degradation, sensitive to radiomimetic agents, and defective in P1 lysogenization. All are able to propagate temperature-sensitive phage better than lon+ parental strains. Mutations that suppress the radiation sensitivity of these strains (sul) also suppress the P1 lysogenization defect, but do not affect mucoidy or the degradation defect.

MeSH Terms
Bacterial Proteins/metabolism Chromosome Mapping Escherichia coli/genetics Galactosidases/metabolism Genotype Glycosaminoglycans/biosynthesis Phenotype Polysaccharides, Bacterial/biosynthesis Temperature
Chemicals
Bacterial Proteins Glycosaminoglycans Polysaccharides, Bacterial Galactosidases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gottesman S
Zipser D
References (22)
22 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1978-02-00
Pages
844-51
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC222096
Subset
IM
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