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Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator.
Science. 1993 Nov 19; 262(5137):1277-80.Sci

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.

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Authors+Show Affiliations

Hughes KT
Department of Microbiology, University of Washington, Seattle 98195.
Gillen KL
No affiliation info available
Semon MJ
No affiliation info available
Karlinsey JE
No affiliation info available

MeSH

Bacterial ProteinsFlagellaFlagellinGene Expression Regulation, BacterialGenes, BacterialGenes, RegulatorModels, BiologicalMorphogenesisRecombinant Fusion ProteinsSalmonella typhimuriumSigma FactorTranscription, Genetic

Pub Type(s)

Comment
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8235660

Citation

Hughes, K T., et al. "Sensing Structural Intermediates in Bacterial Flagellar Assembly By Export of a Negative Regulator." Science (New York, N.Y.), vol. 262, no. 5137, 1993, pp. 1277-80.
Hughes KT, Gillen KL, Semon MJ, et al. Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator. Science. 1993;262(5137):1277-80.
Hughes, K. T., Gillen, K. L., Semon, M. J., & Karlinsey, J. E. (1993). Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator. Science (New York, N.Y.), 262(5137), 1277-80.
Hughes KT, et al. Sensing Structural Intermediates in Bacterial Flagellar Assembly By Export of a Negative Regulator. Science. 1993 Nov 19;262(5137):1277-80. PubMed PMID: 8235660.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator. AU - Hughes,K T, AU - Gillen,K L, AU - Semon,M J, AU - Karlinsey,J E, PY - 1993/11/19/pubmed PY - 1993/11/19/medline PY - 1993/11/19/entrez SP - 1277 EP - 80 JF - Science (New York, N.Y.) JO - Science VL - 262 IS - 5137 N2 - 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. SN - 0036-8075 UR - https://www.unboundmedicine.com/medline/citation/8235660/Sensing_structural_intermediates_in_bacterial_flagellar_assembly_by_export_of_a_negative_regulator_ L2 - https://www.sciencemag.org/cgi/pmidlookup?view=long&pmid=8235660 DB - PRIME DP - Unbound Medicine ER -