Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator
- 19 November 1993
- journal article
- editorial
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 262 (5137) , 1277-1280
- https://doi.org/10.1126/science.8235660
Abstract
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.Keywords
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