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Article

Competition between the Rad50 complex and the Ku heterodimer reveals a role for Exo1 in processing double-strand breaks but not telomeres.

Molecular and cellular biology - 1 Aug 2003

Tomita Kazunori, Matsuura Akira, Caspari Thomas, Carr Antony M, Akamatsu Yufuko, Iwasaki Hiroshi, Mizuno Ken-ichi, Ohta Kunihiro, Uritani Masahiro, Ushimaru Takashi, Yoshinaga Koichi, Ueno Masaru

Abstract excerpt

The Mre11-Rad50-Nbs1(Xrs2) complex and the Ku70-Ku80 heterodimer are thought to compete with each other for binding to DNA ends. To investigate the mechanism underlying this competition, we analyzed both DNA damage sensitivity and telomere overhangs in Schizosaccharomyces pombe rad50-d, rad50-d pku70-d, rad50-d exo1-d, and pku70-d rad50-d exo1-d cells. We found that rad50 exo1 double mutants are more methyl...

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Share to Antigens, Nuclear
Share to Binding, Competitive

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dose-Response Relationship, Radiation

Share to Exodeoxyribonucleases

Share to Fluorescent Antibody Technique, Indirect

Share to Gamma Rays

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Source

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Identifiers

PMID: 12861005
DOI: 10.1128/MCB.23.15.5186-5197.2003
PMCID: PMC165728

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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