DEG PHENOTYPE OF ESCHERICHIA-COLI ION MUTANTS
DEG PHENOTYPE OF ESCHERICHIA-COLI ION MUTANTS
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DOI：
10.1128/jb.133.2.844-851.1978
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发表时间：
1978-01-01
影响因子：
3.2
通讯作者：
ZIPSER, D
中科院分区：
文献类型：
--
作者：
GOTTESMAN, S;ZIPSER, D
DEG是一种降解异常多肽(如无义片段)的大肠杆菌系统，也参与了某些错义蛋白质的降解。β-半乳糖苷酶的错义蛋白和对温度敏感的噬菌体产物似乎都被Deg系统降解。DIG系统中的突变与经典上称为LON或CAPR的突变难以区分；所有靠近proc的MAP都是粘液样的，蛋白质降解有缺陷，对仿射线药物敏感，在P1裂原化方面有缺陷。它们对温度敏感噬菌体的繁殖能力均好于亲本菌株Lon+。抑制这些菌株的辐射敏感性的突变(SUL)也抑制了P1裂原化缺陷，但不影响粘液性或降解缺陷。
Deg, 1 of the E. 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.