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Tethering on the brink: the evolutionarily conserved Mre11-Rad50 complex.

John C Connelly, David R F Leach

Journal: Trends in biochemical sciences 2002;27(8):410-8

PMID: 12151226

Full Text on Elsevier Science View on PubMed

Abstract

Mre11-Rad50 (MR) proteins are encoded by bacteriophage, eubacterial, archeabacterial and eukaryotic genomes, and form a complex with a remarkable protein architecture. This complex is capable of tethering the ends of DNA molecules, possesses a variety of DNA nuclease, helicase, ATPase and annealing activities, and performs a wide range of functions within cells. It is required for meiotic recombination, double-strand break repair, processing of mis-folded DNA structures and maintaining telomere length. This article reviews current knowledge of the structure and enzymatic activities of the MR complex and attempts to integrate biochemical information with the roles of the protein in a cell.

Address: Institute of Cell and Molecular Biology, University of Edinburgh, Kings Buildings, Edinburgh, UK EH9 3JR.
DOI: 10.1016/s0968-0004(02)02144-8

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MeSH Terms: Amino Acid Sequence, Conserved Sequence, Crystallography, DNA Repair, DNA-Binding Proteins, Endodeoxyribonucleases, Evolution, Molecular, Exodeoxyribonucleases, Fungal Proteins, Humans, MRE11 Homologue Protein, Molecular Sequence Data, Protein Conformation, Saccharomyces cerevisiae Proteins, Telomere
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