ArticleNature communications2017
Structural basis of human PCNA sliding on DNA.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Conserved assembly architecture of the essential herpesvirus packaging accessory factor.PLoS pathogens · 2026Article
- Mechanistic diversity of clamp loading at small DNA gaps.The Journal of biological chemistry · 2026Review
- APE1 coordinates its disordered region and metal cofactors to drive genome surveillance.Nucleic acids research · 2026Article
- Bacterial collagenase harnesses collagen geometry for processive cleavage.Nature communications · 2026Article
- Article
- Bacillus subtilis ParB C-terminal lysine residues are essential for dimerization and in vivo function, indicating their roles in DNA sliding.Nucleic acids research · 2026Article
- Conserved assembly architecture of the essential herpesvirus packaging accessory factor.bioRxiv : the preprint server for biology · 2026Article
- Structural insights into the exchange mechanism of a replicative DNA polymerase.Nucleic acids research · 2025Article
- USP1 inhibition: A journey from target discovery to clinical translation.Pharmacology & therapeutics · 2025Review
- Functional asymmetry in processivity clamp proteins.Biophysical journal · 2025Review
- Structural and molecular basis of PCNA-activated FAN1 nuclease function in DNA repair.Nature communications · 2025Article
- A FAN1 point mutation associated with accelerated Huntington's disease progression alters its PCNA-mediated assembly on DNA.Nature communications · 2025Article
- Macromolecular crystallography at Elettra: current and future perspectives.Journal of synchrotron radiation · 2025Article
- The structure of the MutL-CTD:processivity-clamp complex provides insight regarding strand discrimination in non-methyl-directed DNA mismatch repair.Nucleic acids research · 2025Article
- Impact of Optimized Ku-DNA Binding Inhibitors on the Cellular and In Vivo DNA Damage Response.Cancers · 2024Article
- Structure of the E. coli nucleoid-associated protein YejK reveals a novel DNA binding clamp.Nucleic acids research · 2024Article
- Deciphering functional roles of protein succinylation and glutarylation using genetic code expansion.Nature chemistry · 2024Article
- ZNF827 is a single-stranded DNA binding protein that regulates the ATR-CHK1 DNA damage response pathway.Nature communications · 2024Article
- Impact of Asp/Glu-ADP-ribosylation on protein-protein interaction and protein function.Proteomics · 2023Article
- Visualization of direct and diffusion-assisted RAD51 nucleation by full-length human BRCA2 protein.Molecular cell · 2023Article
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7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sliding clamps encircle DNA and tether polymerases and other factors to the genomic template. However, the molecular mechanism of clamp sliding on DNA is unknown. Using crystallography, NMR and molecular dynamics simulations, here we show that the human clamp PCNA recognizes DNA through a double patch of basic residues within the ring channel, arranged in a right-hand spiral that matches the pitch of B-DNA. We propose that PCNA slides by tracking the DNA backbone via a 'cogwheel' mechanism based on short-lived polar interactions, which keep the orientation of the clamp invariant relative to DNA. Mutation of residues at the PCNA-DNA interface has been shown to impair the initiation of DNA synthesis by polymerase δ (pol δ). Therefore, our findings suggest that a clamp correctly oriented on DNA is necessary for the assembly of a replication-competent PCNA-pol δ holoenzyme.
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