The Intriguing Mystery of RPA Phosphorylation in DNA Double-Strand Break Repair.
Genes (Basel)
; 15(2)2024 01 27.
Article
em En
| MEDLINE
| ID: mdl-38397158
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 interactions involving RPA, and how PTMs regulate RPA activity and complex formation in double-strand break repair. There are many holes in our understanding of this research area. We will conclude with perspectives for future research on how RPA PTMs control double-strand break repair in the cell cycle.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
DNA
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Reparo do DNA
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Proteína de Replicação A
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Quebras de DNA de Cadeia Dupla
Limite:
Humans
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article