Gottesman, S., Zipser, D. (February 1978) Deg phenotype of Escherichia coli lon mutants. J Bacteriol, 133 (2). pp. 844-51. ISSN 0021-9193 (Print)0021-9193 (Linking)
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.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | Bacterial Proteins/*metabolism Chromosome Mapping Escherichia coli/*genetics Galactosidases/*metabolism Genotype Glycosaminoglycans/biosynthesis Phenotype Polysaccharides, Bacterial/biosynthesis Temperature |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosome bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosomes, structure and function > chromosome organism description > bacteria > escherichia coli |
| CSHL Authors: | |
| Communities: | CSHL labs |
| Depositing User: | Matt Covey |
| Date: | February 1978 |
| Date Deposited: | 14 Dec 2016 21:56 |
| Last Modified: | 14 Dec 2016 21:56 |
| PMCID: | PMC222096 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/33291 |
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