Fission yeast Mcm10p contains primase activity

doi:10.1074/jbc.M512997200

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Papers In Press, published online ahead of print May 23, 2006
J. Biol. Chem, 10.1074/jbc.M512997200
Submitted on December 6, 2005
Revised on May 4, 2006
Accepted on May 23, 2006

Fission yeast Mcm10p contains primase activity

Karen Fien and Jerard Hurwitz

Program of Molecular Biology, Memorial Sloan-Kettering Cancer Center, New York, NY 10021

Corresponding Author: j-hurwitz{at}ski.mskcc.org

Although Mcm10p is a conserved essential component in eukaryotes required for both the initiation and elongation of DNA chains, its biochemical properties are unknown. Here we report that the fission yeast Mcm10 protein (SpMcm10p) contains primase activity. Primases are enzymes that synthesize RNA primers on single-stranded DNA templates which are extended by DNA polymerases. In keeping with this property, Mcm10p supports oligoribonucleotide synthesis of short RNA primers, preferentially initiating synthesis on template dT, that are extended with dATP by E. coli DNA polymerase I. The C-terminus of Mcm10p synthesizes RNA, but less efficiently than full-length protein at low rNTP levels. Mcm10p homologs contain a C-terminal motif found in proteins that polymerize nucleotides. A point mutant within this motif of SpMcm10p is defective in primer synthesis in vitro, and in vivo this mutant fails to support growth, suggesting that the primase activity of Mcm10p may be essential for cell viability.

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