Bacterial flagellar diversity in the post-genomic era

Mark Pallen; Charles Penn; Roy Chaudhuri

doi:10.1016/j.tim.2005.02.008

Bacterial flagellar diversity in the post-genomic era

Mark Pallen, Charles Penn, Roy Chaudhuri

Biosciences

Research output: Contribution to journal › Review article

75 Citations (Scopus)

Abstract

Flagellar biosynthesis has been studied most thoroughly in laboratory strains of Escherichia coli and Salmonella enterica. However, genome sequencing has uncovered flagellar loci in distantly related bacteria. We have used homology searches to determine how far the E. coli/S. enterica paradigm can be generalised to other flagellar systems. Numerous previously unrecognized homologues of flagellar components were discovered, including novel FIgM, FIgN, FliK and FliO homologues. Homology was found between the FIiK proteins and a molecular ruler, YscP, from a virulence-associated type-III secretion system. Also described is a new family of flagellar proteins, the FIhX proteins, which resemble the cytoplasmic domain of FIhB.

Original language	English
Pages (from-to)	143-149
Number of pages	7
Journal	Trends in Microbiology
Volume	13
Issue number	4
DOIs	https://doi.org/10.1016/j.tim.2005.02.008
Publication status	Published - 1 Apr 2005

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title = "Bacterial flagellar diversity in the post-genomic era",

abstract = "Flagellar biosynthesis has been studied most thoroughly in laboratory strains of Escherichia coli and Salmonella enterica. However, genome sequencing has uncovered flagellar loci in distantly related bacteria. We have used homology searches to determine how far the E. coli/S. enterica paradigm can be generalised to other flagellar systems. Numerous previously unrecognized homologues of flagellar components were discovered, including novel FIgM, FIgN, FliK and FliO homologues. Homology was found between the FIiK proteins and a molecular ruler, YscP, from a virulence-associated type-III secretion system. Also described is a new family of flagellar proteins, the FIhX proteins, which resemble the cytoplasmic domain of FIhB.",

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AU - Penn, Charles

AU - Chaudhuri, Roy

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N2 - Flagellar biosynthesis has been studied most thoroughly in laboratory strains of Escherichia coli and Salmonella enterica. However, genome sequencing has uncovered flagellar loci in distantly related bacteria. We have used homology searches to determine how far the E. coli/S. enterica paradigm can be generalised to other flagellar systems. Numerous previously unrecognized homologues of flagellar components were discovered, including novel FIgM, FIgN, FliK and FliO homologues. Homology was found between the FIiK proteins and a molecular ruler, YscP, from a virulence-associated type-III secretion system. Also described is a new family of flagellar proteins, the FIhX proteins, which resemble the cytoplasmic domain of FIhB.

AB - Flagellar biosynthesis has been studied most thoroughly in laboratory strains of Escherichia coli and Salmonella enterica. However, genome sequencing has uncovered flagellar loci in distantly related bacteria. We have used homology searches to determine how far the E. coli/S. enterica paradigm can be generalised to other flagellar systems. Numerous previously unrecognized homologues of flagellar components were discovered, including novel FIgM, FIgN, FliK and FliO homologues. Homology was found between the FIiK proteins and a molecular ruler, YscP, from a virulence-associated type-III secretion system. Also described is a new family of flagellar proteins, the FIhX proteins, which resemble the cytoplasmic domain of FIhB.

U2 - 10.1016/j.tim.2005.02.008

DO - 10.1016/j.tim.2005.02.008

M3 - Review article

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EP - 149

JO - Trends in Microbiology

JF - Trends in Microbiology

IS - 4

ER -

Bacterial flagellar diversity in the post-genomic era

Abstract

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