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• W2148045256 endingPage "1971" @default.
• W2148045256 startingPage "1959" @default.
• W2148045256 abstract "Double-strand breaks (DSBs) in chromosomal DNA elicit a rapid signaling response through the ATM protein kinase. ATM corresponds to Tel1 in budding yeast. Here we show that the catalytic activity of Tel1 is altered by protein binding at DNA ends via the Mre11-Rad50-Xrs2 (MRX) complex. Like ATM, Tel1 is activated through interaction with the MRX complex and DNA ends. In vivo, Tel1 activation is enhanced in sae2Δ or mre11-3 mutants after camptothecin treatment; both of these mutants are defective in the removal of topoisomerase I from DNA. In contrast, an sae2Δ mutation does not stimulate Tel1 activation after expression of the EcoRI endonuclease, which generates clean DNA ends. In an in vitro system, tethering of Fab fragments to DNA ends inhibits MRX-mediated DNA end processing but enhances Tel1 activation. The mre11-3 mutation abolishes DNA end-processing activity but does not affect the ability to enhance Tel1 activation. These results support a model in which MRX controls Tel1 activation by recognizing protein-bound DNA ends." @default.
• W2148045256 created "2016-06-24" @default.
• W2148045256 creator A5005189404 @default.
• W2148045256 creator A5033422116 @default.
• W2148045256 creator A5039867806 @default.
• W2148045256 creator A5090899284 @default.
• W2148045256 date "2011-05-01" @default.
• W2148045256 modified "2023-10-16" @default.
• W2148045256 title "Activation of Protein Kinase Tel1 through Recognition of Protein-Bound DNA Ends" @default.
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• W2148045256 doi "https://doi.org/10.1128/mcb.05157-11" @default.
• W2148045256 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3133365" @default.
• W2148045256 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21402778" @default.
• W2148045256 hasPublicationYear "2011" @default.
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