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

Autor: Hughes KT; Department of Microbiology, University of Washington, Seattle 98195., Gillen KL, Semon MJ, Karlinsey JE
Jazyk: angličtina
Zdroj: Science (New York, N.Y.) [Science] 1993 Nov 19; Vol. 262 (5137), pp. 1277-80.
DOI: 10.1126/science.8235660
Abstrakt: 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.
Databáze: MEDLINE