Chaperoning RPA during DNA metabolism
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Single-stranded DNA (ssDNA) is widely generated during DNA metabolisms including DNA replication, repair and recombination and is susceptible to digestion by nucleases and secondary structure formation. It is vital for DNA metabolism and genome stability that ssDNA is protected and stabilized, which are performed by the major ssDNA-binding protein, and replication protein A (RPA) in these processes. In addition, RPA-coated ssDNA also serves as a protein–protein-binding platform for coordinating multiple events during DNA metabolisms. However, little is known about whether and how the formation of RPA–ssDNA platform is regulated. Here we highlight our recent study of a novel RPA-binding protein, Regulator of Ty1 transposition 105 (Rtt105) in Saccharomyces cerevisiae, which regulates the RPA–ssDNA platform assembly at replication forks. We propose that Rtt105 functions as an “RPA chaperone” during DNA replication, likely also promoting the assembly of RPA–ssDNA platform in other processes in which RPA plays a critical role.
KeywordsRPA chaperone Rtt105 RPA–ssDNA platform DNA replication Replication stress
This work was supported by grants from NSFC [31725015, 31830048 (QL) and 31671332 (JF)].
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