RT Journal Article
SR Electronic
T1 A new insight into RecA filament regulation by RecX from the analysis of conformation-specific interactions
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2022.03.14.484239
DO 10.1101/2022.03.14.484239
A1 Aleksandr Alekseev
A1 Georgii Pobegalov
A1 Natalia Morozova
A1 Alexey Vedyaykin
A1 Galina Cherevatenko
A1 Alexander Yakimov
A1 Dmitry Baitin
A1 Mikhail Khodorkovskii
YR 2022
UL http://biorxiv.org/content/early/2022/03/14/2022.03.14.484239.abstract
AB RecA protein mediates homologous recombination repair in bacteria through assembly of long helical filaments on single-stranded DNA (ssDNA) in an ATP dependent manner. RecX, an important negative regulator of RecA, is known to inhibit RecA activity by stimulating the disassembly of RecA nucleoprotein filaments. Here we use a single-molecule approach to address the regulation of (E. coli) RecA-ssDNA filaments by RecX (E. coli) within the framework of distinct conformational states of RecA-ssDNA filament. Our findings revealed that RecX effectively binds the inactive conformation of RecA-ssDNA filaments and slows down the transition to the active state. Results of this work provide new mechanistic insights into the RecX-RecA interactions and highlight the importance of conformational transitions of RecA filaments as an additional level of regulation of its biological activity.Competing Interest StatementThe authors have declared no competing interest.