The Intriguing Mystery of RPA Phosphorylation in DNA Double-Strand Break Repair.

ABSTRACT: Human Replication Protein A (RPA) was historically discovered as one of the six components needed to reconstitute simian virus 40 DNA replication from purified components. RPA is now known to be involved in all DNA metabolism pathways that involve single-stranded DNA (ssDNA). Heterotrimeric RPA comprises several domains connected by flexible linkers and is heavily regulated by post-translational modifications (PTMs). The structure of RPA has been challenging to obtain. Various structural methods have been applied, but a complete understanding of RPA's flexible structure, its function, and how it is regulated by PTMs has yet to be obtained. This review will summarize recent literature concerning how RPA is phosphorylated in the cell cycle, the structural analysis of RPA, DNA and protein int

SUBMITTER: Fousek-Schuller VJ 

PROVIDER: S-EPMC10888239 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature