Escherichia coli K-12 has two distinguishable PriA-PriB replication restart pathways.
DNA repair
DNA replication
SOS response
homologous recombination
replication restart
Journal
Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028
Informations de publication
Date de publication:
10 2021
10 2021
Historique:
revised:
17
08
2021
received:
01
07
2021
accepted:
19
08
2021
pubmed:
24
8
2021
medline:
22
2
2022
entrez:
23
8
2021
Statut:
ppublish
Résumé
In Escherichia coli, PriA, PriB, PriC, and DnaT proteins mediate three pathways for Replication Restart called PriA-PriB, PriA-PriC, and PriC. PriA is crucial for two of the three pathways. Its absence leads to slow growth, high basal levels of SOS expression, poorly partitioning nucleoids, UV sensitivity, and recombination deficiency. PriA has ATPase and helicase activities and interacts with PriB, DnaT, and single-stranded DNA-binding protein (SSB). priA300 (K230R) and priA301 (C479Y) have no phenotype as single mutants, but each phenocopy a priA-null mutant combined with ∆priB. This suggested that the two priA mutations affected the helicase activity that is required for the PriA-PriC pathway. To further test this, the biochemical activities of purified PriA300 and PriA301 were examined. As expected, PriA300 lacks ATPase and helicase activities but retains the ability to interact with PriB. PriA301, however, retains significant PriB-stimulated helicase activity even though PriA301 interactions with PriB and DNA are weakened. A PriA300,301 variant retains only the ability to interact with DNA in vitro and phenocopies the priA-null phenotype in vivo. This suggests that there are two biochemically and genetically distinct PriA-PriB pathways. One uses PriB-stimulated helicase activity to free a region of ssDNA and the other uses helicase-independent remodeling activity.
Identifiants
pubmed: 34423481
doi: 10.1111/mmi.14802
pmc: PMC8541903
mid: NIHMS1735178
doi:
Substances chimiques
DNA, Bacterial
0
DNA-Binding Proteins
0
DnaT protein, E coli
0
Escherichia coli Proteins
0
PriB protein, E coli
0
PriC protein, E coli
146312-41-6
priA protein, E coli
EC 3.6.1.-
DNA Helicases
EC 3.6.4.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
1140-1150Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM098885
Pays : United States
Informations de copyright
© 2021 John Wiley & Sons Ltd.
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