ParA-like protein uses nonspecific chromosomal DNA binding to partition protein complexes.

Recent data have shown that plasmid partitioning Par-like systems are used by some bacterial cells to control localization of protein complexes. Here we demonstrate that one of these homologs, PpfA, uses nonspecific chromosome binding to separate cytoplasmic clusters of chemotaxis proteins upon divi...

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Main Authors: Roberts, M, Wadhams, G, Hadfield, K, Tickner, S, Armitage, J
Format: Journal article
Language:English
Published: 2012
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author Roberts, M
Wadhams, G
Hadfield, K
Tickner, S
Armitage, J
author_facet Roberts, M
Wadhams, G
Hadfield, K
Tickner, S
Armitage, J
author_sort Roberts, M
collection OXFORD
description Recent data have shown that plasmid partitioning Par-like systems are used by some bacterial cells to control localization of protein complexes. Here we demonstrate that one of these homologs, PpfA, uses nonspecific chromosome binding to separate cytoplasmic clusters of chemotaxis proteins upon division. Using fluorescent microscopy and point mutations, we show dynamic chromosome binding and Walker-type ATPase activity are essential for cluster segregation. The N-terminal domain of a cytoplasmic chemoreceptor encoded next to ppfA is also required for segregation, probably functioning as a ParB analog to control PpfA ATPase activity. An orphan ParA involved in segregating protein clusters therefore uses a similar mechanism to plasmid-segregating ParA/B systems and requires a partner protein for function. Given the large number of genomes that encode orphan ParAs, this may be a common mechanism regulating segregation of proteins and protein complexes.
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spelling oxford-uuid:fe1cb298-83ca-4a39-94cc-75250fd560a52022-03-27T13:33:52ZParA-like protein uses nonspecific chromosomal DNA binding to partition protein complexes.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:fe1cb298-83ca-4a39-94cc-75250fd560a5EnglishSymplectic Elements at Oxford2012Roberts, MWadhams, GHadfield, KTickner, SArmitage, JRecent data have shown that plasmid partitioning Par-like systems are used by some bacterial cells to control localization of protein complexes. Here we demonstrate that one of these homologs, PpfA, uses nonspecific chromosome binding to separate cytoplasmic clusters of chemotaxis proteins upon division. Using fluorescent microscopy and point mutations, we show dynamic chromosome binding and Walker-type ATPase activity are essential for cluster segregation. The N-terminal domain of a cytoplasmic chemoreceptor encoded next to ppfA is also required for segregation, probably functioning as a ParB analog to control PpfA ATPase activity. An orphan ParA involved in segregating protein clusters therefore uses a similar mechanism to plasmid-segregating ParA/B systems and requires a partner protein for function. Given the large number of genomes that encode orphan ParAs, this may be a common mechanism regulating segregation of proteins and protein complexes.
spellingShingle Roberts, M
Wadhams, G
Hadfield, K
Tickner, S
Armitage, J
ParA-like protein uses nonspecific chromosomal DNA binding to partition protein complexes.
title ParA-like protein uses nonspecific chromosomal DNA binding to partition protein complexes.
title_full ParA-like protein uses nonspecific chromosomal DNA binding to partition protein complexes.
title_fullStr ParA-like protein uses nonspecific chromosomal DNA binding to partition protein complexes.
title_full_unstemmed ParA-like protein uses nonspecific chromosomal DNA binding to partition protein complexes.
title_short ParA-like protein uses nonspecific chromosomal DNA binding to partition protein complexes.
title_sort para like protein uses nonspecific chromosomal dna binding to partition protein complexes
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