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PMID: 15309560 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

MRE11/RAD50/NBS1: complex activities.

Chromosoma ·Vol. 113 ·No. 4 ·2004-10-00 ·Pages 157-66

Assenmacher N, Hopfner KP

Abstract

The MRE11/RAD50/NBS1 complex (Mre11 complex) is a central player in most aspects of the cellular response to DNA double-strand breaks, including homologous recombination, non-homologous end joining, telomere maintenance and DNA damage checkpoint activation. Several of these findings are explained by the unusual enzymatic activities and macromolecular structure of the Mre11 complex. The Mre11 complex possesses an ATP-stimulated nuclease to process heterogeneous DNA ends and long coiled-coil tails to link DNA ends and/or sister chromatids. However, the mechanistic role of the Mre11 complex in checkpoint activation has been unclear until recently. New data suggest that the Mre11 complex can directly activate the ATM checkpoint kinase at DNA breaks. These findings, together with newly determined functional interactions, identify the Mre11 complex as an architectural and mechanistic keystone of cellular response events emerging from DNA breaks.

MeSH Terms
Acid Anhydride Hydrolases Ataxia Telangiectasia Mutated Proteins Cell Cycle Proteins/chemistry,genetics,metabolism,physiology Chromosome Breakage DNA Helicases/physiology DNA Repair Enzymes/chemistry,genetics,metabolism DNA Replication DNA-Binding Proteins/chemistry,genetics,metabolism,physiology Deoxyribonucleases/physiology Humans MRE11 Homologue Protein Nuclear Proteins/chemistry,genetics,metabolism Protein Serine-Threonine Kinases/physiology Tumor Suppressor Proteins/physiology
Chemicals
Cell Cycle Proteins DNA-Binding Proteins MRE11 protein, human NBN protein, human Nuclear Proteins Tumor Suppressor Proteins ATM protein, human Ataxia Telangiectasia Mutated Proteins Protein Serine-Threonine Kinases Deoxyribonucleases MRE11 Homologue Protein Acid Anhydride Hydrolases Rad50 protein, human DNA Helicases DNA Repair Enzymes
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Assenmacher Nora
Gene Center, University of Munich, Feodor-Lynen-Str. 25, 81377 Munich, Germany.
Hopfner Karl-Peter
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Article Info
Journal
Chromosoma
Abbr.
Chromosoma
ISSN
0009-5915
DOI
10.1007/s00412-004-0306-4
Published
2004-10-00
Epub
2004-00-10
Pages
157-66
Language
English
Region
Austria
NLM ID
2985138R
Subset
IM
External Links
PubMed source DOI: 10.1007/s00412-004-0306-4 View journal details
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