Human claspin is a ring-shaped DNA-binding protein with high affinity to branched DNA structures.
Claspin is an essential protein for the ATR-dependent activation of the DNA replication checkpoint response in Xenopus and human cells. Here we describe the purification and characterization of human Claspin. The protein has a ring-like structure and binds with high affinity to branched DNA molecules. These findings suggest that Claspin may be a component of the replication ensemble and plays a role in the replication checkpoint by directly associating with replication forks and with the various branched DNA structures likely to form at stalled replication forks because of DNA damage.
Sar
Funda
F
Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599, USA.
Lindsey-Boltz
Laura A
LA
Subramanian
Deepa
D
Croteau
Deborah L
DL
Hutsell
Stephanie Q
SQ
Griffith
Jack D
JD
Sancar
Aziz
A
D048868:Adaptor Proteins, Signal Transducing; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D004247:DNA / Q000737:chemistry / Q000648:ultrastructure; D004261:DNA Replication / Q000502:physiology*; D006801:Humans; D008854:Microscopy, Electron; D009690:Nucleic Acid Conformation; D011485:Protein Binding / Q000235:genetics; D020836:Protein Structure, Quaternary; D014981:Xenopus; D029867:Xenopus Proteins
D048868:Adaptor Proteins, Signal Transducing; C416368:CLSPN protein, Xenopus; C488158:CLSPN protein, human; D002352:Carrier Proteins; D029867:Xenopus Proteins; D004247:DNA