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Post-transcriptional regulation of bacterial motility by aconitase proteins

Post-transcriptional regulation of bacterial motility by aconitase proteins
Post-transcriptional regulation of bacterial motility by aconitase proteins

Escherichia coli and Bacillus subtilis aconitases can act as iron and oxidative stress-responsive post-transcriptional regulators. Here, it is shown that a Salmonella enterica serovar Typhimurium LT2 acnB mutant exhibits impaired binding to the surface of J774 macrophage-like cells. Proteomic analyses were used to investigate further the binding defect of the acnB mutant. These revealed that the levels of the flagellum protein FliC were much lower for the acnB mutant. This strain was correspondingly less motile and possessed fewer flagella than either the parental strain or the acnA and acnAB mutants. The acnB lesion did not alter fliC transcription, nor did apo-AcnB select the fliC transcript from a library of S. enterica transcripts; thus, the effect of AcnB on FliC is indirect. Evidence is presented to show that apo-AcnB regulates FliC synthesis via interaction with the ftsH transcript to decrease the intracellular levels of FtsH. The lower levels of FtsH protease activity then influence sigma32, DnaK and, ultimately, FliC production.

ATP-Dependent Proteases, Aconitate Hydratase, Animals, Bacterial Adhesion, Bacterial Proteins, Cell Line, Escherichia coli Proteins, Flagellin, Gene Expression Regulation, Bacterial, Genes, Bacterial, Macrophages, Membrane Proteins, Mice, Microscopy, Electron, Movement, Mutation, Protein Biosynthesis, Proteome, RNA Processing, Post-Transcriptional, Salmonella typhimurium, Journal Article, Research Support, Non-U.S. Gov't
0950-382X
1817-1826
Tang, Yue
9158ac9d-2ecb-45c0-a2a3-383bd78b9b29
Guest, John R
9d52f305-d25f-4c7e-9ed0-7014398aaa6e
Artymiuk, Peter J
c0535846-f7a9-43b3-a0ab-4bfca9fde212
Read, Robert C
b5caca7b-0063-438a-b703-7ecbb6fc2b51
Green, Jeffrey
bd38753d-70c3-4327-9893-090ffb2b15ea
Tang, Yue
9158ac9d-2ecb-45c0-a2a3-383bd78b9b29
Guest, John R
9d52f305-d25f-4c7e-9ed0-7014398aaa6e
Artymiuk, Peter J
c0535846-f7a9-43b3-a0ab-4bfca9fde212
Read, Robert C
b5caca7b-0063-438a-b703-7ecbb6fc2b51
Green, Jeffrey
bd38753d-70c3-4327-9893-090ffb2b15ea

Tang, Yue, Guest, John R, Artymiuk, Peter J, Read, Robert C and Green, Jeffrey (2004) Post-transcriptional regulation of bacterial motility by aconitase proteins. Molecular Microbiology, 51 (6), 1817-1826. (doi:10.1111/j.1365-2958.2003.03954.x).

Record type: Article

Abstract

Escherichia coli and Bacillus subtilis aconitases can act as iron and oxidative stress-responsive post-transcriptional regulators. Here, it is shown that a Salmonella enterica serovar Typhimurium LT2 acnB mutant exhibits impaired binding to the surface of J774 macrophage-like cells. Proteomic analyses were used to investigate further the binding defect of the acnB mutant. These revealed that the levels of the flagellum protein FliC were much lower for the acnB mutant. This strain was correspondingly less motile and possessed fewer flagella than either the parental strain or the acnA and acnAB mutants. The acnB lesion did not alter fliC transcription, nor did apo-AcnB select the fliC transcript from a library of S. enterica transcripts; thus, the effect of AcnB on FliC is indirect. Evidence is presented to show that apo-AcnB regulates FliC synthesis via interaction with the ftsH transcript to decrease the intracellular levels of FtsH. The lower levels of FtsH protease activity then influence sigma32, DnaK and, ultimately, FliC production.

Full text not available from this repository.

More information

e-pub ahead of print date: 13 February 2004
Published date: March 2004
Keywords: ATP-Dependent Proteases, Aconitate Hydratase, Animals, Bacterial Adhesion, Bacterial Proteins, Cell Line, Escherichia coli Proteins, Flagellin, Gene Expression Regulation, Bacterial, Genes, Bacterial, Macrophages, Membrane Proteins, Mice, Microscopy, Electron, Movement, Mutation, Protein Biosynthesis, Proteome, RNA Processing, Post-Transcriptional, Salmonella typhimurium, Journal Article, Research Support, Non-U.S. Gov't

Identifiers

Local EPrints ID: 416423
URI: https://eprints.soton.ac.uk/id/eprint/416423
ISSN: 0950-382X
PURE UUID: ac913c3c-20b9-43e8-bc64-598bc63b409e
ORCID for Robert C Read: ORCID iD orcid.org/0000-0002-4297-6728

Catalogue record

Date deposited: 15 Dec 2017 17:30
Last modified: 14 Mar 2019 01:36

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