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 |
Externí odkaz: |
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