Histone deposition at the replication fork: a matter of urgency.
In this issue of Molecular Cell, Ye et al. provide a biological rationale for rapid histone deposition behind the replication fork. They show that defects in nucleosome assembly lead to DNA double-strand breaks and S phase arrest. Their results have important implications for the maintenance of genome integrity in proliferating cells.
Verreault
Alain
A
Cancer Research UK, London Research Institute, Clare Hall Laboratories, Blanche Lane, South Mimms, EN6 3LD, Herts, United Kingdom.
D064007:Ataxia Telangiectasia Mutated Proteins; D018797:Cell Cycle Proteins; D056504:Chromatin Assembly Factor-1; D002868:Chromosomal Proteins, Non-Histone; D004249:DNA Damage; D004261:DNA Replication / Q000502:physiology*; D004268:DNA-Binding Proteins / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D006801:Humans; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D025521:Tumor Suppressor Proteins
D018797:Cell Cycle Proteins; D056504:Chromatin Assembly Factor-1; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D006657:Histones; D025521:Tumor Suppressor Proteins; C576324:ATM protein, human; C576597:ATR protein, human; D064007:Ataxia Telangiectasia Mutated Proteins; D017346:Protein Serine-Threonine Kinases