大肠杆菌lon突变体的Deg表型
Deg phenotype of Escherichia coli lon mutants.
作者信息
Gottesman S, Zipser D
出版信息
J Bacteriol. 1978 Feb;133(2):844-51. doi: 10.1128/jb.133.2.844-851.1978.
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.
摘要
大肠杆菌降解异常多肽（如无义片段）的系统之一Deg，也参与某些错义蛋白的降解。β-半乳糖苷酶的错义蛋白和温度敏感型噬菌体产物似乎都由Deg系统降解。Deg系统中的突变与经典称为lon或capR的突变无法区分；所有突变都定位在proC附近，都是黏液型的，在蛋白质降解方面有缺陷，对放射模拟剂敏感，并且在P1溶原化方面有缺陷。所有这些突变体都比lon +亲代菌株能更好地繁殖温度敏感型噬菌体。抑制这些菌株辐射敏感性的突变（sul）也抑制P1溶原化缺陷，但不影响黏液性或降解缺陷。
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