Relief of ParB autoinhibition by parS DNA catalysis and recycling of ParB by CTP hydrolysis promote bacterial centromere assembly.

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License: CC BY-NC 4.0
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Serval ID
serval:BIB_20D31F118858
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Relief of ParB autoinhibition by parS DNA catalysis and recycling of ParB by CTP hydrolysis promote bacterial centromere assembly.
Journal
Science advances
Author(s)
Antar H., Soh Y.M., Zamuner S., Bock F.P., Anchimiuk A., Rios P.L., Gruber S.
ISSN
2375-2548 (Electronic)
ISSN-L
2375-2548
Publication state
Published
Issued date
08/10/2021
Peer-reviewed
Oui
Volume
7
Number
41
Pages
eabj2854
Language
english
Notes
Publication types: Journal Article
Publication Status: ppublish
Abstract
Three-component ParABS systems are widely distributed factors for plasmid partitioning and chromosome segregation in bacteria. ParB acts as adaptor protein between the 16-base pair centromeric parS DNA sequences and the DNA segregation proteins ParA and Smc (structural maintenance of chromosomes). Upon cytidine triphosphate (CTP) and parS DNA binding, ParB dimers form DNA clamps that spread onto parS-flanking DNA by sliding, thus assembling the so-called partition complex. We show here that CTP hydrolysis is essential for efficient chromosome segregation by ParABS but largely dispensable for Smc recruitment. Our results suggest that CTP hydrolysis contributes to partition complex assembly via two mechanisms. It promotes ParB unloading from DNA to limit the extent of ParB spreading, and it recycles off-target ParB clamps to allow for parS retargeting, together super-concentrating ParB near parS. We also propose a model for clamp closure involving a steric clash when binding ParB protomers to opposing parS half sites.
Pubmed
Web of science
Create date
12/10/2021 8:35
Last modification date
23/02/2022 6:36
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