FlgM Is secreted by the flagellar export apparatus in Bacillus subtilis

Rebecca A. Calvo, Daniel B. Kearns

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The bacterial flagellum is assembled from over 20 structural components, and flagellar gene regulation is morphogenetically coupled to the assembly state by control of the anti-sigma factor FlgM. In the Gram-negative bacterium Salmonella enterica, FlgM inhibits late-class flagellar gene expression until the hook-basal body structural intermediate is completed and FlgM is inhibited by secretion from the cytoplasm. Here we demonstrate that FlgM is also secreted in the Gram-positive bacterium Bacillus subtilis and is degraded extracellularly by the proteases Epr and WprA. We further demonstrate that, like in S. enterica, the structural genes required for the flagellar hook-basal body are required for robust activation of σD-dependent gene expression and efficient secretion of FlgM. Finally, we determine that FlgM secretion is strongly enhanced by, but does not strictly require, hook-basal body completion and instead demands a minimal subset of flagellar proteins that includes the FliF/FliG basal body proteins, the flagellar type III export apparatus components FliO, FliP, FliQ, FliR, FlhA, and FlhB, and the substrate specificity switch regulator FliK.

Original languageEnglish (US)
Pages (from-to)81-91
Number of pages11
JournalJournal of bacteriology
Volume197
Issue number1
DOIs
StatePublished - Jan 1 2015

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Basal Bodies
Bacillus subtilis
Salmonella enterica
Gene Components
Sigma Factor
Gene Expression
Flagella
Gram-Positive Bacteria
Substrate Specificity
Gram-Negative Bacteria
Cytoplasm
Proteins
Peptide Hydrolases
Genes

Cite this

FlgM Is secreted by the flagellar export apparatus in Bacillus subtilis. / Calvo, Rebecca A.; Kearns, Daniel B.

In: Journal of bacteriology, Vol. 197, No. 1, 01.01.2015, p. 81-91.

Research output: Contribution to journalArticle

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