Xrs2p regulates Mre11p translocation to the nucleus and plays a role in telomere elongation and meiotic recombination.

doi:10.1091/mbc.e04-09-0782

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Article

Xrs2p regulates Mre11p translocation to the nucleus and plays a role in telomere elongation and meiotic recombination.

Molecular biology of the cell - 1 Feb 2005

Tsukamoto Yasumasa, Mitsuoka Chikako, Terasawa Masahiro, Ogawa Hideyuki, Ogawa Tomoko

Abstract excerpt

The Mre11-Rad50-Xrs2 (MRX) protein complex plays pivotal roles in meiotic recombination, repair of damaged DNA, telomere elongation, and cell cycle checkpoint control. Xrs2p is known to be essential for all the functions of the complex, but its role in the complex has not been clearly elucidated. A 32-amino acid region near the C terminus of Xrs2p was identified as an Mre11p-binding site. No more function of...

Topics

Alleles
Amino Acid Sequence
Binding Sites
Cell Nucleus
Cytoplasm
DNA Repair
Endodeoxyribonucleases
Exodeoxyribonucleases
Immunohistochemistry
Meiosis
Point Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Precipitin Tests

Protein Binding

Protein Structure, Tertiary

Recombination, Genetic

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Telomere

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Identifiers

PMID: 15548595
DOI: 10.1091/mbc.e04-09-0782
PMCID: PMC545897

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