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Papers In Press, published online ahead of print January 22, 2002
Biochemistry & Molecular Biology, Univ. of Maryland, Baltimore, MD 21201
Corresponding Author: aluchang{at}umaryland.edu
The MutY homolog (MYH) is responsible for removing adenines misincorporated on template DNA strand containing G or 7,8-dihydro-8-oxo-guanine (8-oxoG) and thus preventing G:C to T:A mutations. Human MYH has been shown to interact physically with human proliferating cell nuclear antigen (hPCNA). Here, we report that similar interaction between SpMYH and SpPCNA occurs in the fission yeast Schizosaccharomyces pombe. Binding of SpMYH to SpPCNA was not observed when phenylalanine-444 in the PCNA binding motif of SpMYH was replaced with alanine. The F444A mutant of SpMYH expressed in yeast cells had normal adenine glycosylase and DNA binding activities. However, expression of this mutant form of SpMYH in a SpMYHD cell could not reduce the mutation frequency of the cell to the normal level. Moreover, SpMYH interacted with hPCNA and SpPCNA interacted with hMYH but not with F518AF519A mutant hMYH containing mutations in its PCNA binding motif. While the SpMYH
J. Biol. Chem, 10.1074/jbc.M111739200
Submitted on December 10, 2001
Revised on January 16, 2002
Accepted on January 18, 2002
Functional interaction of MutY homolog (MYH) with proliferating cell nuclear antigen (PCNA) in fission yeast, Schizosaccharomyces pombe
cells expressing hMYH had partially reduced mutation frequency, the F518AF519A mutant hMYH could not reduce the mutation frequency of SpMYH{dalta} cells. Thus, the interaction between SpMYH and SpPCNA is important for SpMYH biological function in mutation avoidance.
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