Multistep loading of a DNA sliding clamp onto DNA by replication factor C.
DNA repair
DNA replication
PCNA
S. cerevisiae
molecular biophysics
structural biology
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
08 08 2022
08 08 2022
Historique:
received:
28
02
2022
accepted:
07
07
2022
entrez:
8
8
2022
pubmed:
9
8
2022
medline:
11
8
2022
Statut:
epublish
Résumé
The DNA sliding clamp proliferating cell nuclear antigen (PCNA) is an essential co-factor for many eukaryotic DNA metabolic enzymes. PCNA is loaded around DNA by the ATP-dependent clamp loader replication factor C (RFC), which acts at single-stranded (ss)/double-stranded DNA (dsDNA) junctions harboring a recessed 3' end (3' ss/dsDNA junctions) and at DNA nicks. To illuminate the loading mechanism we have investigated the structure of RFC:PCNA bound to ATPγS and 3' ss/dsDNA junctions or nicked DNA using cryogenic electron microscopy. Unexpectedly, we observe open and closed PCNA conformations in the RFC:PCNA:DNA complex, revealing that PCNA can adopt an open, planar conformation that allows direct insertion of dsDNA, and raising the question of whether PCNA ring closure is mechanistically coupled to ATP hydrolysis. By resolving multiple DNA-bound states of RFC:PCNA we observe that partial melting facilitates lateral insertion into the central channel formed by RFC:PCNA. We also resolve the Rfc1 N-terminal domain and demonstrate that its single BRCT domain participates in coordinating DNA prior to insertion into the central RFC channel, which promotes PCNA loading on the lagging strand of replication forks in vitro. Combined, our data suggest a comprehensive and fundamentally revised model for the RFC-catalyzed loading of PCNA onto DNA.
Identifiants
pubmed: 35939393
doi: 10.7554/eLife.78253
pii: 78253
pmc: PMC9359705
doi:
pii:
Substances chimiques
Proliferating Cell Nuclear Antigen
0
Saccharomyces cerevisiae Proteins
0
Adenosine Triphosphate
8L70Q75FXE
DNA
9007-49-2
Replication Protein C
EC 3.6.4.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NCI NIH HHS
ID : P30 CA008748
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM107239
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM132081
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM127428
Pays : United States
Informations de copyright
© 2022, Schrecker, Castaneda et al.
Déclaration de conflit d'intérêts
MS, JC, SD, CK, DR, RH Authors declare that they have no competing interests
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