Single-molecule observation of ATP-independent SSB displacement by RecO in Deinococcus radiodurans.

Abstract:

:Deinococcus radiodurans (DR) survives in the presence of hundreds of double-stranded DNA (dsDNA) breaks by efficiently repairing such breaks. RecO, a protein that is essential for the extreme radioresistance of DR, is one of the major recombination mediator proteins in the RecA-loading process in the RecFOR pathway. However, how RecO participates in the RecA-loading process is still unclear. In this work, we investigated the function of drRecO using single-molecule techniques. We found that drRecO competes with the ssDNA-binding protein (drSSB) for binding to the freely exposed ssDNA, and efficiently displaces drSSB from ssDNA without consuming ATP. drRecO replaces drSSB and dissociates it completely from ssDNA even though drSSB binds to ssDNA approximately 300 times more strongly than drRecO does. We suggest that drRecO facilitates the loading of RecA onto drSSB-coated ssDNA by utilizing a small drSSB-free space on ssDNA that is generated by the fast diffusion of drSSB on ssDNA.

journal_name

Elife

journal_title

eLife

authors

Hwang J,Kim JY,Kim C,Park S,Joo S,Kim SK,Lee NK

doi

10.7554/eLife.50945

subject

Has Abstract

pub_date

2020-04-16 00:00:00

issn

2050-084X

pii

50945

journal_volume

9

pub_type

杂志文章

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