The R215W mutation in NBS1 impairs gamma-H2AX binding and affects DNA repair: molecular bases for the severe phenotype of 657del5/R215W Nijmegen breakage syndrome patients

Biochem Biophys Res Commun. 2008 May 9;369(3):835-40. doi: 10.1016/j.bbrc.2008.02.129. Epub 2008 Mar 6.

Abstract

Nijmegen breakage syndrome (NBS) is a genetic disorder characterized by chromosomal instability and hypersensitivity to ionising radiation. Compound heterozygous 657del5/R215W NBS patients display a clinical phenotype more severe than the majority of NBS patients homozygous for the 657del5 mutation. The NBS1 protein, mutated in NBS patients, contains a FHA/BRCT domain necessary for the DNA-double strand break (DSB) damage response. Recently, a second BRCT domain has been identified, however, its role is still unknown. Here, we demonstrate that the R215W mutation in NBS1 impairs histone gamma-H2AX binding after induction of DNA damage, leading to a delay in DNA-DSB rejoining. Molecular modelling reveals that the 215 residue of NBS1 is located between the two BRCT domains, affecting their relative orientation that appears critical for gamma-H2AX binding. Present data represent the first evidence for the role of NBS1 tandem BRCT domains in gamma-H2AX recognition, and could explain the severe phenotype observed in 657del5/R215W NBS patients.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution / genetics
  • Arginine / chemistry
  • Arginine / genetics
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / genetics*
  • Cell Cycle Proteins / metabolism*
  • DNA Breaks, Double-Stranded
  • DNA Repair / genetics*
  • Histones / metabolism*
  • Humans
  • Molecular Sequence Data
  • Mutation, Missense*
  • Nijmegen Breakage Syndrome / diagnosis*
  • Nijmegen Breakage Syndrome / genetics
  • Nijmegen Breakage Syndrome / metabolism
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics*
  • Nuclear Proteins / metabolism*
  • Phenotype
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Deletion
  • Severity of Illness Index
  • Transfection
  • Tryptophan / chemistry
  • Tryptophan / genetics

Substances

  • Cell Cycle Proteins
  • H2AX protein, human
  • Histones
  • NBN protein, human
  • Nuclear Proteins
  • Tryptophan
  • Arginine