Learning our ABCs: Rad50 directs MRN repair functions via adenylate kinase activity from the conserved ATP binding cassette

Mol Cell. 2007 Mar 23;25(6):789-91. doi: 10.1016/j.molcel.2007.03.004.

Abstract

In groundbreaking work, Bhaskara et al. (2007) demonstrate in a recent issue of Molecular Cell that the Mre11/Rad50/Nbs1 (MRN) complex harbors distinct, yet chemically related, ATPase and adenylate kinase catalytic activities that together orchestrate multiple requisite MRN functional and conformational states in dsDNA break repair sensing and signaling with general implications for ABC ATPases.

Publication types

  • Comment

MeSH terms

  • Acid Anhydride Hydrolases
  • Adenylate Kinase / metabolism*
  • Archaeal Proteins / metabolism*
  • Cell Cycle Proteins / metabolism*
  • Cystic Fibrosis Transmembrane Conductance Regulator / chemistry
  • Cystic Fibrosis Transmembrane Conductance Regulator / metabolism
  • DNA Repair Enzymes / metabolism*
  • DNA-Binding Proteins / metabolism*
  • Endodeoxyribonucleases / metabolism*
  • Exodeoxyribonucleases / metabolism*
  • Humans
  • MRE11 Homologue Protein
  • Nuclear Proteins / metabolism*
  • Protein Conformation
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • Archaeal Proteins
  • Cell Cycle Proteins
  • DNA-Binding Proteins
  • MRE11 protein, human
  • NBN protein, human
  • Nuclear Proteins
  • RAD50 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • Adenylate Kinase
  • Endodeoxyribonucleases
  • Exodeoxyribonucleases
  • MRE11 Homologue Protein
  • MRE11 protein, S cerevisiae
  • Mre11 protein, archaeal
  • Rad50 protein, archaeal
  • Acid Anhydride Hydrolases
  • RAD50 protein, human
  • DNA Repair Enzymes