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Science 19 November 1993:
Vol. 262. no. 5137, pp. 1277 - 1280
DOI: 10.1126/science.8235660
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Articles

Science, Vol 262, Issue 5137, 1277-1280
Copyright © 1993 by American Association for the Advancement of Science

articles

Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator

KT Hughes, KL Gillen, MJ Semon, and JE Karlinsey

Department of Microbiology, University of Washington, Seattle 98195.

The ability of a regulatory protein to sense the integrity of the bacterial flagellar structure was investigated. In response to a defective hook-basal body complex, the anti-sigma 28 FlgM protein inhibits flagellin transcription. In cells with a functional hook-basal body complex, the flagellin genes are transcribed normally and the FlgM protein is expelled into the growth medium. In strains with a defective hook-basal body structure, FlgM is absent from the media. The presence of flagellin protein in the media is substantially reduced in strains carrying a FlgM-LacZ protein fusion, suggesting that the fusion is blocking the flagellar export apparatus. These results suggest that the FlgM protein assesses the integrity of the flagellar hook-basal body complex by itself being a substrate for export by the flagellar-specific export apparatus.


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   Abstract »    Full Text »
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