Evidence map›Paper›PMID 21127055›Full record

ArticleThe Journal of biological chemistry2011

Molecular basis of BACH1/FANCJ recognition by TopBP1 in DNA replication checkpoint control.

Charles Chung Yun Leung, Zihua Gong, Junjie Chen, J N Mark Glover

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

40 citing papers in PubMed, 66 citations in OpenAlex.

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  4. Crystal structure of the folded domains of Xrs2 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 2025
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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

4 authors at 2 institutions in 2 countries.

Charles Chung Yun LeungDepartment of Biochemistry, School of Molecular and Systems Medicine, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Zihua Gong
Junjie Chen
J N Mark Glover
The University of Texas MD Anderson Cancer Center · USUniversity of Alberta · CA

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Analysis of BRCA1 Function in DNA RepairR01CA089239 · NCI · YALE UNIVERSITY · PI CHEN, JUNJIE · 2001 to 2015
$3.7M
Howard Hughes Medical InstituteNCI NIH HHS CA089239NCI NIH HHS CA92584NCI NIH HHS P01 CA092584NCI NIH HHS R01 CA089239
6 · The paper itself

Abstract

The diverse roles of TopBP1 in DNA replication and checkpoint signaling are associated with the scaffolding ability of TopBP1 to initiate various protein-protein interactions. The recognition of the BACH1/FANCJ helicase by TopBP1 is critical for the activation of the DNA replication checkpoint at stalled replication forks and is facilitated by the C-terminal tandem BRCT7/8 domains of TopBP1 and a phosphorylated Thr(1133) binding motif in BACH1. Here we provide the structural basis for this interaction through analysis of the x-ray crystal structures of TopBP1 BRCT7/8 both free and in complex with a BACH1 phospho-peptide. In contrast to canonical BRCT-phospho-peptide recognition, TopBP1 BRCT7/8 undergoes a dramatic conformational change upon BACH1 binding such that the two BRCT repeats pivot about the central BRCT-BRCT interface to provide an extensive and deep peptide-binding cleft. Additionally, we provide the first structural mechanism for Thr(P) recognition among BRCT domains. Together with systematic mutagenesis studies, we highlight the role of key contacts in governing the unique specificity of the TopBP1-BACH1 interaction.

Indexed as

Amino Acid MotifsAmino Acid SubstitutionBasic-Leucine Zipper Transcription FactorsCarrier ProteinsCrystallography, X-RayDNADNA-Binding ProteinsDNA HelicasesDNA ReplicationFanconi Anemia Complementation Group ProteinsHumansMutagenesisNuclear ProteinsPhosphorylationProtein Structure, QuaternaryStructure-Activity RelationshipBACH1 protein, humanBasic-Leucine Zipper Transcription FactorsCarrier ProteinsDNADNA-Binding ProteinsDNA HelicasesFanconi Anemia Complementation Group ProteinsNuclear ProteinsTOPBP1 protein, human

Identifiers

PMID21127055
PMCPMC3039391
OpenAlexW2016373103

What OpenQuestion holds

Textmetadata
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.