Structural Insight Into the Function of DnaB Helicase in Bacterial DNA Replication.
DNA replication
DnaB helicase
allosteric regulation
conformational change
coupling
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
04 Sep 2024
04 Sep 2024
Historique:
revised:
16
07
2024
received:
25
01
2024
accepted:
26
08
2024
medline:
4
9
2024
pubmed:
4
9
2024
entrez:
4
9
2024
Statut:
aheadofprint
Résumé
In bacteria, chromosome replication is achieved by the coordinations of more than a dozen replisome enzymes. Replication initiation protein DnaA melts DNA duplex at replication origin (oriC) and forms a replication bubble, followed by loading of helicase DnaB with the help of loader protein DnaC. Then the DnaB helicase unwinds the dsDNA and supports the priming of DnaG and the polymerizing of DNA polymerase. The DnaB helicase functions as a platform coupling unwinding, priming, and polymerizing events. The multiple roles of DnaB helicase are underlined by its distinctive architecture and dynamics conformations. In this review, we will discuss the assembling of DnaB hexamer and the conformational changes upon binding of various partners, DnaB in states of closed dilated (CD), closed constricted (CC), closed helical (CH), and open helical (OH) are discussed. These multiple interfaces among DnaB and partners are potential targets for inhibitors design and novel peptide antibiotics development.
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Science and Technology Department of Sichuan Province
ID : 2022YFSY0028
Organisme : National Natural Science Foundation of China, NSFC
ID : 31470742
Organisme : National Natural Science Foundation of China, NSFC
ID : U1432102
Organisme : National Natural Science Foundation of China, NSFC
ID : 31700664
Organisme : National Natural Science Foundation of China, NSFC
ID : 31270783
Organisme : 100 Talents Program of the Chinese Academy of Sciences
Informations de copyright
© 2024 Wiley Periodicals LLC.
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