Spatial coupling between DNA replication and mismatch repair in Caulobacter crescentus.
Amino Acid Motifs
Base Pair Mismatch
Caulobacter crescentus
/ genetics
DNA Helicases
/ metabolism
DNA Mismatch Repair
DNA Replication
DNA-Directed DNA Polymerase
/ metabolism
Multienzyme Complexes
/ metabolism
MutL Proteins
/ metabolism
MutS DNA Mismatch-Binding Protein
/ chemistry
S Phase
/ genetics
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
06 04 2021
06 04 2021
Historique:
accepted:
09
02
2021
revised:
19
01
2021
received:
10
07
2020
pubmed:
8
3
2021
medline:
13
5
2021
entrez:
7
3
2021
Statut:
ppublish
Résumé
The DNA mismatch repair (MMR) process detects and corrects replication errors in organisms ranging from bacteria to humans. In most bacteria, it is initiated by MutS detecting mismatches and MutL nicking the mismatch-containing DNA strand. Here, we show that MMR reduces the appearance of rifampicin resistances more than a 100-fold in the Caulobacter crescentus Alphaproteobacterium. Using fluorescently-tagged and functional MutS and MutL proteins, live cell microscopy experiments showed that MutS is usually associated with the replisome during the whole S-phase of the C. crescentus cell cycle, while MutL molecules may display a more dynamic association with the replisome. Thus, MMR components appear to use a 1D-scanning mode to search for rare mismatches, although the spatial association between MutS and the replisome is dispensible under standard growth conditions. Conversely, the spatial association of MutL with the replisome appears as critical for MMR in C. crescentus, suggesting a model where the β-sliding clamp licences the endonuclease activity of MutL right behind the replication fork where mismatches are generated. The spatial association between MMR and replisome components may also play a role in speeding up MMR and/or in recognizing which strand needs to be repaired in a variety of Alphaproteobacteria.
Identifiants
pubmed: 33677508
pii: 6157100
doi: 10.1093/nar/gkab112
pmc: PMC8034640
doi:
Substances chimiques
Multienzyme Complexes
0
DNA synthesome
EC 2.7.7.-
DNA-Directed DNA Polymerase
EC 2.7.7.7
MutL Proteins
EC 3.6.1.3
MutS DNA Mismatch-Binding Protein
EC 3.6.1.3
DNA Helicases
EC 3.6.4.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3308-3321Informations de copyright
© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.
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