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PMID: 7932752 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Caulobacter flagellar function, but not assembly, requires FliL, a non-polarly localized membrane protein present in all cell types.

Journal of molecular biology ·Vol. 243 ·No. 2 ·1994-10-21 ·Pages 227-44

Jenal U, White J, Shapiro L

Abstract

Caulobacter crescentus has a single polar flagellum, which is assembled in the predivisional cell. Known flagellar genes encode structural and regulatory components that are required for flagellar assembly and function. These genes are organized in several classes which form a transcriptional regulatory hierarchy. A member of the Class II genes, the fliLM operon, encodes homologs of the Escherichia coli flagellar switch protein, FliM, and a protein with a hitherto unknown function, FliL. We report here that flagellar rotation requires the FliL protein. In-frame deletions in the chromosomal copy of the fliL gene result in cells that form a flagellum but are non-motile. The FliL protein was found to be associated with the inner membrane and to be present in all cell types. This is the first report of a Caulobacter crescentus protein that is essential for motility but is not spatially restricted to the region of the flagellar basal body. Although FliL is required for flagellar function, it is not part of the transcriptional hierarchy, supporting the hypothesis that, as is the case for the enterics, the regulatory hierarchy responds to assembly cues rather than directly to the expression of flagellar proteins.

MeSH Terms
Amino Acid Sequence Antibodies, Bacterial/immunology Antibody Specificity Bacterial Proteins/genetics,immunology,physiology Base Sequence Caulobacter crescentus/chemistry,physiology,ultrastructure Cell Fractionation Escherichia coli Proteins Flagella/chemistry,physiology,ultrastructure Immunoblotting Membrane Proteins/physiology Microscopy, Electron Molecular Sequence Data Movement/physiology Precipitin Tests Sequence Deletion
Chemicals
Antibodies, Bacterial Bacterial Proteins Escherichia coli Proteins FliL protein, E coli Membrane Proteins FliM protein, Bacteria FliL protein, Bacteria
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Jenal U
Department of Developmental Biology Beckman Center, Stanford University School of Medicine, CA 94305-5427.
White J
Shapiro L
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
1994-10-21
Pages
227-44
Language
English
Region
England
NLM ID
2985088R
Subset
IM
Grants
NIGMS NIH HHS · GM32506 · United States
Databases
GENBANK
M85232
Corrections
ErratumIn
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