MUTANTS IN DISULFIDE BOND FORMATION THAT DISRUPT FLAGELLAR ASSEMBLY IN ESCHERICHIA-COLI

被引：223
作者：
DAILEY, FE
BERG, HC
机构：
[1] Cellular/Developmental Biology Dept., Harvard University, Cambridge
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1993年 / 90卷 / 03期
关键词：
MOTILITY; CHEMOTAXIS; PROTEIN FOLDING;
D O I：
10.1073/pnas.90.3.1043
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
We report the isolation and characterization of Escherichia coli mutants (dsbB) that fail to assemble functional flagella unless cystine is present. Flagellar basal bodies obtained from these mutants are missing the L and P rings. This defect in assembly appears to result from an inability to form a disulfide bond in the P-ring protein (FlgI). Cystine suppresses this defect in dsbB strains. We also show that dsbA strains [Bardwell, J. C. A., McGovern, K. & Beckwith, J. (1991) Cell 67, 581-589] fail to assemble P rings, apparently from a similar failure in disulfide bond formation. However, cystine does not completely suppress this defect in dsbA strains. Thus, disulfide bond formation in FlgI is essential for assembly. DsbA likely puts in that bond directly, whereas the DsbB product(s) play a role in oxidizing DsbA, so that it can be active.
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页码：1043 / 1047
页数：5
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