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Article

Effect of amino acid substitutions in the rad50 ATP binding domain on DNA double strand break repair in yeast.

The Journal of biological chemistry - 28 Jan 2005

Chen Ling, Trujillo Kelly M, Van Komen Stephen, Roh Dong Hyun, Krejci Lumir, Lewis L Kevin, Resnick Michael A, Sung Patrick, Tomkinson Alan E

Abstract excerpt

The Saccharomyces cerevisiae Rad50-Mre11-Xrs2 complex plays a central role in the cellular response to DNA double strand breaks. Rad50 has a globular ATPase head domain with a long coiled-coil tail. DNA binding by Rad50 is ATP-dependent and the Rad50-Mre11-Xrs2 complex possesses DNA unwinding and endonuclease activities that are regulated by ATP. Here we have examined the role of the Rad50 Walker type A ATP...

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Identifiers

PMID: 15546877
DOI: 10.1074/jbc.M410192200

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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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Effect of amino acid substitutions in the rad50 ATP binding domain on DNA double strand break repair in yeast.PMID 15546877Read ↗

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