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Binding of MCM-interacting proteins to ATP-binding site in MCM6

Authors Hosoi A, Sakairi T, Ishimi Y

Received 11 September 2015

Accepted for publication 15 December 2015

Published 9 March 2016 Volume 2016:7 Pages 31—40

DOI https://doi.org/10.2147/RRB.S96215

Checked for plagiarism Yes

Review by Single-blind

Peer reviewers approved by Dr Venkatesh Kota

Peer reviewer comments 2

Editor who approved publication: Professor Zvi Kelman

Atsutoshi Hosoi, Taku Sakairi, Yukio Ishimi

Graduate School of Science and Engineering, Ibaraki University, Mito, Ibaraki, Japan

Abstract: The function of MCM2–7 complex that is a DNA helicase in DNA replication may be regulated by various MCM-interacting proteins, including CDC45, RPA, TIM, TIPIN, Claspin, MCM10, and MCM-BP. It has been shown by immunoprecipitation that human MCM6 interacts with all these proteins in coexpressed insect cells. To determine the region in MCM6 to interact with these proteins, we prepared various truncated forms of MCM6 and examined the interaction of these MCM6 fragments with the MCM-interacting proteins. All these proteins bound to C-terminal half of MCM6, and CDC45, RPA2, TIM, TIPIN, MCM-BP, and MCM10 bound to the fragments containing ATP-binding motifs. CDC45 and RPA2 bound to the smallest fragment containing Walker motif A. Only MCM-BP is bound to the N-terminal half of MCM6. Site-directed mutagenesis study suggests that hydrophobic interaction is involved in the interaction of MCM6 with CDC45 and TIM. These results suggest a possibility that MCM-interacting proteins regulate MCM2–7 function by modulating the ATP-binding ability of the MCM2–7.

Keywords: DNA helicase, DNA replication, checkpoint, MCM2–7 proteins

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