Article
Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks, maintains checkpoint arrest, and influences DNA repair in fission yeast.
Molecular and cellular biology - 1 Jul 2004
Nakamura Toru M, Du Li-Lin, Redon Christophe, Russell Paul
Abstract excerpt
Mammalian ATR and ATM checkpoint kinases modulate chromatin structures near DNA breaks by phosphorylating a serine residue in the carboxy-terminal tail SQE motif of histone H2AX. Histone H2A is similarly regulated in Saccharomyces cerevisiae. The phosphorylated forms of H2AX and H2A, known as gamma-H2AX and gamma-H2A, are thought to be important for DNA repair, although their evolutionarily conserved roles are...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
