2025-06-23 九州大学
図1 複製起点oriCにおける複製開始機構(正常)と阻害時のレスキュー機構
<関連情報>
- https://www.kyushu-u.ac.jp/ja/researches/view/1286
- https://www.kyushu-u.ac.jp/f/62122/25_0623_01.pdf
- https://elifesciences.org/reviewed-preprints/103340v2
プリモソームタンパク質PriCは、DnaA-DnaB相互作用のステップを迂回することで、oriCにおけるDnaBヘリカーゼのローディングのために複製開始ストレスを救う Primosomal protein PriC rescues replication initiation stress by bypassing the DnaA-DnaB interaction step for DnaB helicase loading at oriC
Ryusei Yoshida,Kazuma Korogi,Qinfei Wu,Shogo Ozaki,Tsutomu Katayama
eLife Published:May 29, 2025
DOI:https://doi.org/10.7554/eLife.103340.2
Abstract
In Escherichia coli, replisome and replication fork assembly is initiated by DnaB helicase loading at the chromosomal origin oriC via its interactions with the DnaA initiator and the DnaC helicase loader. Upon replication fork arrest, the replisome including DnaB dissociates from the stalled fork. Replication fork progression is rescued by primosomal protein PriA- or PriC-dependent pathway in which PriA and PriC promote reloading of DnaB in different mechanisms. However, the mechanism responsible for rescue of blocked replication initiation at oriC remains unclear. Here, we found that PriC rescued blocked replication initiation in cells expressing an initiation-specific DnaC mutant, in mutant cells defective in DnaA-DnaB interactions, and in cells containing truncated oriC sequence variants. PriC rescued DnaB loading at oriC even in the absence of Rep helicase, a stimulator of the PriC-dependent replication fork restart pathway. These and results of in vitro reconstituted assays concordantly suggest that this initiation-specific rescue mechanism provides a bypass of the DnaA-DnaB interaction for DnaB loading by PriC-promoted loading of DnaB to the unwound oriC region. These findings expand understanding of mechanisms sustaining the robustness of replication initiation and specific roles for PriC in the genome maintenance.
