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Human Claspin Is a Ring-shaped DNA-binding Protein with High Affinity to Branched DNA Structures

Year: 2004
Type: article
Abstract: 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.
DOI: 10.1074/jbc.m405793200
Authors: Funda Sar, Laura A. Lindsey-Boltz, Deepa Subramanian, Deborah L. Croteau, Stephanie Q. Hutsell, Jack D. Griffith, Aziz Sancar
Language: English
Open Access status: hybrid
Estimated APC paid: $3,430
Awards: DNA Excision Repair and DNA Damage Checkpoints, G2774293502, DNA-Protein Interactions at the Replication Fork, G4172127056, FOLDING AND STABILITY OF CIRCULARLY PERMUTED PROTEINS, G694257262
OpenAlex ID: W2068764175
FWCI: 2.743
Cites: 29
Cited by: 84
Related to: 10