Evidence map›Paper›PMID 17308348›Full record

ArticleNucleic acids research2007

The C-terminal domain of yeast PCNA is required for physical and functional interactions with Cdc9 DNA ligase.

Sangeetha Vijayakumar, Brian R Chapados, Kristina H Schmidt, Richard D Kolodner, John A Tainer, Alan E Tomkinson

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

49 citing papers in PubMed, 77 citations in OpenAlex.

  1. Ribonucleotide errors, RNase HII, and ribonucleotide excision repair.Critical reviews in biochemistry and molecular biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
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  9. Unorthodox PCNA Binding by Chromatin Assembly Factor 1.International journal of molecular sciences · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. The PCNA interaction motifs revisited: thinking outside the PIP-box.Cellular and molecular life sciences : CMLS · 2019
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Eukaryotic DNA Replication Fork.Annual review of biochemistry · 2017
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Sangeetha VijayakumarRadiation Oncology Research Laboratory, Department of Radiation Oncology and The Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD 21201-1509, USA.
Brian R Chapados
Kristina H Schmidt
Richard D Kolodner
John A Tainer
Alan E Tomkinson
Ludwig Cancer Research · USUniversity of California, San Diego · USScripps Research Institute · USUniversity of Maryland, Baltimore · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
ENZYMOLOGY OF MISMATCH REPAIR IN YEASTR01GM050006 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Richard D Kolodner · 1994 to 2026
$10.5M
FEN1 STRUCTURES AND HUMAN GENOME STABILITYR01CA081967 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 1999 to 2013
$4.2M
ROLES OF DNA LIGASE I IN MAMMALIAN DNA METABOLISMR01GM057479 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI TOMKINSON, ALAN E · 2000 to 2017
$3.7M
NCI NIH HHS CA081967NCI NIH HHS P01 CA092584NCI NIH HHS P01 CA92584NCI NIH HHS R01 CA081967NIGMS NIH HHS GM57479NIGMS NIH HHS R01 GM050006NIGMS NIH HHS R01 GM057479
6 · The paper itself

Abstract

There is compelling evidence that proliferating cell nuclear antigen (PCNA), a DNA sliding clamp, co-ordinates the processing and joining of Okazaki fragments during eukaryotic DNA replication. However, a detailed mechanistic understanding of functional PCNA:ligase I interactions has been incomplete. Here we present the co-crystal structure of yeast PCNA with a peptide encompassing the conserved PCNA interaction motif of Cdc9, yeast DNA ligase I. The Cdc9 peptide contacts both the inter-domain connector loop (IDCL) and residues near the C-terminus of PCNA. Complementary mutational and biochemical results demonstrate that these two interaction interfaces are required for complex formation both in the absence of DNA and when PCNA is topologically linked to DNA. Similar to the functionally homologous human proteins, yeast RFC interacts with and inhibits Cdc9 DNA ligase whereas the addition of PCNA alleviates inhibition by RFC. Here we show that the ability of PCNA to overcome RFC-mediated inhibition of Cdc9 is dependent upon both the IDCL and the C-terminal interaction interfaces of PCNA. Together these results demonstrate the functional significance of the beta-zipper structure formed between the C-terminal domain of PCNA and Cdc9 and reveal differences in the interactions of FEN-1 and Cdc9 with the two PCNA interfaces that may contribute to the co-ordinated, sequential action of these enzymes.

Indexed as

Amino Acid SequenceBinding SitesCrystallography, X-RayDNADNA Ligase ATPDNA LigasesFungal ProteinsModels, MolecularMolecular Sequence DataPeptidesProliferating Cell Nuclear AntigenProtein Structure, TertiaryReplication Protein CDNADNA Ligase ATPDNA LigasesFungal ProteinsLIG1 protein, humanPeptidesProliferating Cell Nuclear AntigenReplication Protein C

Identifiers

PMID17308348
PMCPMC1865074
OpenAlexW1986084992

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.