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Papers In Press, published online ahead of print August 8, 2002
J. Biol. Chem, 10.1074/jbc.M206194200
Submitted on June 21, 2002
Revised on August 7, 2002
Accepted on August 7, 2002

A proteomics approach to identify PCNA binding proteins in human cell lysates: identification of the human CHL12/RFCs2-5 complex as a novel PCNA binding protein

Satoshi Ohta, Yasushi Shiomi, Katsunori Sugimoto, Chikashi Obuse, and Toshiki Tsurimoto

Graduate School of Biological Science, Nara Institute of Science and Technology, Ikoma, Nara 630-0101

Corresponding Author: turimoto{at}bs.aist-nara.ac.jp

PCNA, a eukaryotic DNA replication factor, functions not only as a processivity factor for DNA polymerase d, but also as a binding partner for multiple other factors. To understand its broad significance, we have carried out systematic studies of PCNA binding proteins by a combination of affinity chromatography and mass-spectrometric analyses. We detected more than 20 specific protein bands of various intensities in fractions bound to PCNA-fixed resin from human cell lysates, and determined their peptide sequences by liquid chromatography and tandem mass-spectrometry (LC/MS/MS). A search with human protein databases identified 12 reported PCNA binding proteins from both cytoplasmic (S100 lysate) and nuclear extracts with substantial significance, and four more solely from the nuclear preparation. CHL12, a factor involved in checkpoint response and chromosome cohesion, was a novel example found in both lysates. Further studies with recombinant proteins demonstrated that CHL12 and small subunits of replication factor C form a complex, which interacts with PCNA.


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