Bacterial actin: architecture of the ParMRC plasmid DNA partitioning complex.

The R1 plasmid employs ATP-driven polymerisation of the actin-like protein ParM to move newly replicated DNA to opposite poles of a bacterial cell. This process is essential for ensuring accurate segregation of the low-copy number plasmid and is the best characterised example of DNA partitioning in...

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Κύριοι συγγραφείς: Salje, J, Löwe, J
Μορφή: Journal article
Γλώσσα:English
Έκδοση: 2008
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author Salje, J
Löwe, J
author_facet Salje, J
Löwe, J
author_sort Salje, J
collection OXFORD
description The R1 plasmid employs ATP-driven polymerisation of the actin-like protein ParM to move newly replicated DNA to opposite poles of a bacterial cell. This process is essential for ensuring accurate segregation of the low-copy number plasmid and is the best characterised example of DNA partitioning in prokaryotes. In vivo, ParM only forms long filaments when capped at both ends by attachment to a centromere-like region parC, through a small DNA-binding protein ParR. Here, we present biochemical and electron microscopy data leading to a model for the mechanism by which ParR-parC complexes bind and stabilise elongating ParM filaments. We propose that the open ring formed by oligomeric ParR dimers with parC DNA wrapped around acts as a rigid clamp, which holds the end of elongating ParM filaments while allowing entry of new ATP-bound monomers. We propose a processive mechanism by which cycles of ATP hydrolysis in polymerising ParM drives movement of ParR-bound parC DNA. Importantly, our model predicts that each pair of plasmids will be driven apart in the cell by just a single double helical ParM filament.
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spelling oxford-uuid:5197112b-e32c-4e49-bfd4-908719cee5872022-03-26T16:20:28ZBacterial actin: architecture of the ParMRC plasmid DNA partitioning complex.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:5197112b-e32c-4e49-bfd4-908719cee587EnglishSymplectic Elements at Oxford2008Salje, JLöwe, JThe R1 plasmid employs ATP-driven polymerisation of the actin-like protein ParM to move newly replicated DNA to opposite poles of a bacterial cell. This process is essential for ensuring accurate segregation of the low-copy number plasmid and is the best characterised example of DNA partitioning in prokaryotes. In vivo, ParM only forms long filaments when capped at both ends by attachment to a centromere-like region parC, through a small DNA-binding protein ParR. Here, we present biochemical and electron microscopy data leading to a model for the mechanism by which ParR-parC complexes bind and stabilise elongating ParM filaments. We propose that the open ring formed by oligomeric ParR dimers with parC DNA wrapped around acts as a rigid clamp, which holds the end of elongating ParM filaments while allowing entry of new ATP-bound monomers. We propose a processive mechanism by which cycles of ATP hydrolysis in polymerising ParM drives movement of ParR-bound parC DNA. Importantly, our model predicts that each pair of plasmids will be driven apart in the cell by just a single double helical ParM filament.
spellingShingle Salje, J
Löwe, J
Bacterial actin: architecture of the ParMRC plasmid DNA partitioning complex.
title Bacterial actin: architecture of the ParMRC plasmid DNA partitioning complex.
title_full Bacterial actin: architecture of the ParMRC plasmid DNA partitioning complex.
title_fullStr Bacterial actin: architecture of the ParMRC plasmid DNA partitioning complex.
title_full_unstemmed Bacterial actin: architecture of the ParMRC plasmid DNA partitioning complex.
title_short Bacterial actin: architecture of the ParMRC plasmid DNA partitioning complex.
title_sort bacterial actin architecture of the parmrc plasmid dna partitioning complex
work_keys_str_mv AT saljej bacterialactinarchitectureoftheparmrcplasmiddnapartitioningcomplex
AT lowej bacterialactinarchitectureoftheparmrcplasmiddnapartitioningcomplex