RPA-like single-stranded DNA-binding protein complexes including CST serve as specialized processivity factors for polymerases

• Published in: Current opinion in structural biology Vol. 81; p. 102611
• Main Authors: Barbour, Alexandra T., Wuttke, Deborah S.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.08.2023
• Subjects: DNA Replication; DNA, Single-Stranded; Humans; Nucleotidyltransferases - genetics; Protein Binding; Saccharomyces cerevisiae - metabolism; Telomere - metabolism; Telomere-Binding Proteins - chemistry; Telomere-Binding Proteins - genetics; Telomere-Binding Proteins - metabolism; OB fold; RPA; wHTH; RD; CST; DBD; PARP; ssDNA
• ISSN: 0959-440X; 1879-033X; 1879-033X
• DOI: 10.1016/j.sbi.2023.102611

Telomeres and other single-stranded regions of the genome require specialized management to maintain stability and for proper progression of DNA metabolism pathways. Human Replication Protein A and CTC1-STN1-TEN1 are structurally similar heterotrimeric protein complexes that have essential ssDNA-binding roles in DNA replication, repair, and telomeres. Yeast and ciliates have related ssDNA-binding proteins with strikingly conserved structural features to these human heterotrimeric protein complexes. Recent breakthrough structures have extended our understanding of these commonalities by illuminating a common mechanism used by these proteins to act as processivity factors for their partner polymerases through their ability to manage ssDNA. •CST and RPA share similar protein structure architecture.•Human, Saccharomyces cerevisiae and Tetrahymena all have RPA-like protein complexes.•RPA-like proteins use an ssDNA threading mechanism to act as processivity factors.