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Nucleic Acids Research, 2000, Vol. 28, No. 5 1237-1244
© 2000 Oxford University Press

Protein sequences conserved in prokaryotic aminoacyl-tRNA synthetases are important for the activity of the processivity factor of human mitochondrial DNA polymerase

José A. Carrodeguas and Daniel F. Bogenhagen*

Department of Pharmacological Sciences, State University of New York at Stony Brook, Stony Brook, NY 11794-8651, USA

Previous studies have shown that the small subunit of Xenopus DNA polymerase {gamma} (pol {gamma}B) acts as a processivity factor to stimulate the 140 kDa catalytic subunit of human DNA polymerase {gamma}. A putative human pol {gamma}B initially identified by analysis of DNA sequence had not been shown to be functional, and appeared to be an incomplete clone. In this paper, we report the cloning of full-length human and mouse pol {gamma}B. Both human and mouse pol {gamma}B proteins were expressed in their mature forms, without their apparent mitochondrial localization signals, and shown to stimulate processivity of the recombinant catalytic subunit of human pol {gamma}A. Deletion analysis of human pol {gamma}B indicated that blocks of sequence conserved with prokaryotic class II aminoacyl-tRNA synthetases are necessary for activity and inter­action with human pol {gamma}A. Purification of DNA pol {gamma} from HeLa cells indicated that both proteins are associated in vivo.

* To whom correspondence should be addressed. Tel: +1 516 444 3068; Fax: +1 516 444 3218; Email: dan@pharm.sunysb.edu


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