Publication Date:
1993-11-19
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hughes, K T -- Gillen, K L -- Semon, M J -- Karlinsey, J E -- GM43149/GM/NIGMS NIH HHS/ -- T32-GM07270/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 19;262(5137):1277-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235660" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Proteins/genetics/*metabolism
;
Flagella/metabolism/*ultrastructure
;
Flagellin/*genetics
;
Gene Expression Regulation, Bacterial
;
Genes, Bacterial
;
Genes, Regulator
;
Models, Biological
;
Morphogenesis
;
Recombinant Fusion Proteins/metabolism
;
Salmonella typhimurium/genetics/growth & development/metabolism/*ultrastructure
;
Sigma Factor/genetics/metabolism
;
*Transcription, Genetic
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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