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Functional and molecular insights into the role of Sae2 C-terminus in the activation of MRX endonuclease.

Nucleic acids research - 11 Dec 2024

Colombo Chiara Vittoria, Casari Erika, Gnugnoli Marco, Corallo Flavio, Tisi Renata, Longhese Maria Pia

Abstract excerpt

The yeast Sae2 protein, known as CtIP in mammals, once phosphorylated at Ser267, stimulates the endonuclease activity of the Mre11-Rad50-Xrs2 (MRX) complex to cleave DNA ends that possess hairpin structures or protein blocks, such as the Spo11 transesterase or trapped topoisomerases. Stimulation of the Mre11 endonuclease by Sae2 depends on a Rad50-Sae2 interaction, but the mechanism by which this is achieved...

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DNA Cleavage
Endodeoxyribonucleases
Endonucleases
Enzyme Activation
Exodeoxyribonucleases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phosphorylation

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

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PMID: 39558159
DOI: 10.1093/nar/gkae1049
PMCID: PMC11662671

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Functional and molecular insights into the role of Sae2 C-terminus in the activation of MRX endonuclease.PMID 39558159Read ↗

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Molecular insights into the activation of Mre11-Rad50 endonuclease activity by Sae2/CtIPSemantic proximity Read ↗

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