Mutations in the Escherichia coli surE gene increase isoaspartyl accumulation in a strain lacking the pcm repair methyltransferase but suppress stress-survival phenotypes
被引:24
作者:
Visick, JE
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机构:Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA
Visick, JE
Ichikawa, JK
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机构:Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA
Ichikawa, JK
Clarke, S
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机构:
Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USAUniv Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA
Clarke, S
[1
]
机构:
[1] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA
[2] Univ Calif Los Angeles, Inst Mol Biol, Los Angeles, CA 90095 USA
protein repair;
isoaspartate;
protein methyltransferase;
stationary phase;
stress;
survival;
D O I:
10.1016/S0378-1097(98)00362-0
中图分类号:
Q93 [微生物学];
学科分类号:
071005 ;
100705 ;
摘要:
The Escherichia coli surE gene is co-transcribed with pcm, encoding the L-isoaspartyl protein repair methyltransferase, and is highly conserved among both the Eubacteria and the Archaea; however, no biochemical function has yet been identified for this gene. Isoaspartyl accumulation during stationary phase was much higher in a pcm surE double mutant than in either single mutant, suggesting that the two genes may represent two parallel pathways by which E. coli can respond to protein damage. A null mutation in surE also suppressed stress-survival defects previously observed in a pcm mutant strain, providing further evidence for an interaction between the two gene products. (C) 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.