Dpb11 facilitates the colocalization of Mec1-Ddc2 with its activators on gapped DNA.

Emily C Beckwitt, Gabriella N L Chua, Shixin Liu, Michael E O'Donnell

Abstract read

In one paragraph

Article in Cell reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

Corrections and comments

Update of
Molecular interplay between the DNA damage checkpoint kinase Mec1-Ddc2 and its activator Dpb11 on gapped DNA.2025

5 · Who and what money

Authors and funding

4 authors.

Emily C BeckwittLaboratory of DNA Replication, The Rockefeller University, New York, NY, USA.

Gabriella N L ChuaLaboratory of DNA Replication, The Rockefeller University, New York, NY, USA; Howard Hughes Medical Institute, The Rockefeller University, New York, NY, USA.

Shixin LiuLaboratory of Nanoscale Biophysics and Biochemistry, The Rockefeller University, New York, NY, USA. Electronic address: shixinliu@rockefeller.edu.

Michael E O'DonnellLaboratory of DNA Replication, The Rockefeller University, New York, NY, USA; Howard Hughes Medical Institute, The Rockefeller University, New York, NY, USA. Electronic address: odonnel@rockefeller.edu.

Funding

Biochemistry of Eukaryotic Replication Fork and DNA RepairR35GM148159 · NIGMS · ROCKEFELLER UNIVERSITY · PI MICHAEL E O'DONNELL · 2023 to 2026

$1.7M

Biophysical Determinants of the Nucleosome as an Activity Center for Chromatin RegulatorsR01GM149862 · NIGMS · ROCKEFELLER UNIVERSITY · PI Shixin Liu · 2023 to 2026

$1.4M

NIGMS NIH HHS R01 GM149862NIGMS NIH HHS R35 GM148159

6 · The paper itself

Abstract

The eukaryotic DNA damage and replication stress checkpoint is initiated by activation of the apical kinase complex ATR-ATRIP on RPA-coated ssDNA. In Saccharomyces cerevisiae, the Mec1-Ddc2 (hATR-ATRIP) activator and checkpoint mediator Dpb11 (hTopBP1) is recruited to the 9-1-1 checkpoint clamp (another Mec1-Ddc2 activator) at 5' ss-dsDNA junctions. It remains unclear how Mec1-Ddc2 encounters its activators on damaged DNA due to their differential DNA binding preferences. Using real-time single-molecule imaging, we show that Dpb11 binds to ssDNA directly and localizes to ss-dsDNA junctions in an RPA-dependent manner. Furthermore, Dpb11 recruits Mec1-Ddc2 to ss-dsDNA junctions. Single-molecule force spectroscopy was used to demonstrate that Dpb11 forms bridges on ssDNA, both alone and in the presence of RPA, reducing the end-to-end distance of gapped DNA. These data support a model in which Dpb11 facilitates Mec1-Ddc2 colocalization with its activators directly by recruiting Mec1-Ddc2 to gap junctions and indirectly by decreasing the effective gap length.

Indexed as

Cell Cycle ProteinsDNA, FungalIntracellular Signaling Peptides and ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA DamageDNA, Single-StrandedProtein BindingReplication Protein ACell Cycle ProteinsDNA, FungalDNA, Single-StrandedDPB11 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeProtein Serine-Threonine KinasesReplication Protein ASaccharomyces cerevisiae ProteinsATR-ATRIPcell cycle checkpointCP: molecular biologyDNA damage responseDpb11Mec1-Ddc2replication stresssingle-molecule microscopyTopBP1

Identifiers

PMID42441399

DOI10.1016/j.celrep.2026.117660

PMCPMC13539869

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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.