
Replication Checkpoint Kinase Cds1 Regulates Recombinational Repair Protein Rad60
Author(s) -
Michael N. Boddy,
Paul Shanahan,
W. Hayes McDonald,
Antonia López-Girona,
Eishi Noguchi,
John R. Yates,
Paul Russell
Publication year - 2003
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.23.16.5939-5946.2003
Subject(s) - biology , checkpoint kinase 2 , g2 m dna damage checkpoint , origin recognition complex , microbiology and biotechnology , genetics , postreplication repair , homologous recombination , dna repair , cell cycle checkpoint , kinase , protein kinase a , eukaryotic dna replication , nucleotide excision repair , cell cycle , dna , gene , protein serine threonine kinases
Genome integrity is protected by Cds1 (Chk2), a checkpoint kinase that stabilizes arrested replication forks. How Cds1 accomplishes this task is unknown. We report that Cds1 interacts with Rad60, a protein required for recombinational repair in fission yeast. Cds1 activation triggers Rad60 phosphorylation and nuclear delocalization. A Rad60 mutant that inhibits regulation by Cds1 renders cells specifically sensitive to replication fork arrest. Genetic and biochemical studies indicate that Rad60 functions codependently with Smc5 and Smc6, subunits of an SMC (structural maintenance of chromosomes) complex required for recombinational repair. These studies indicate that regulation of Rad60 is an important part of the replication checkpoint response controlled by Cds1. We propose that control of Rad60 regulates recombination events at stalled forks.