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Molecular and Cellular Biology, June 1999, p. 4039-4046, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Accessory Subunit of Xenopus laevis Mitochondrial DNA Polymerase gamma  Increases Processivity of the Catalytic Subunit of Human DNA Polymerase gamma  and Is Related to Class II Aminoacyl-tRNA Synthetases

José A. Carrodeguas,1 Ryuji Kobayashi,2 Susan E. Lim,3 William C. Copeland,3 and Daniel F. Bogenhagen1,*

Department of Pharmacological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-86511; Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 117242; and Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 277093

Received 11 December 1998/Returned for modification 20 January 1999/Accepted 10 March 1999

Peptide sequences obtained from the accessory subunit of Xenopus laevis mitochondrial DNA (mtDNA) polymerase gamma  (pol gamma ) were used to clone the cDNA encoding this protein. Amino-terminal sequencing of the mitochondrial protein indicated the presence of a 44-amino-acid mitochondrial targeting sequence, leaving a predicted mature protein with 419 amino acids and a molecular mass of 47.3 kDa. This protein is associated with the larger, catalytic subunit in preparations of active mtDNA polymerase. The small subunit exhibits homology to its human, mouse, and Drosophila counterparts. Interestingly, significant homology to glycyl-tRNA synthetases from prokaryotic organisms reveals a likely evolutionary relationship. Since attempts to produce an enzymatically active recombinant catalytic subunit of Xenopus DNA pol gamma  have not been successful, we tested the effects of adding the small subunit of the Xenopus enzyme to the catalytic subunit of human DNA pol gamma  purified from baculovirus-infected insect cells. These experiments provide the first functional evidence that the small subunit of DNA pol gamma  stimulates processive DNA synthesis by the human catalytic subunit under physiological salt conditions.

* Corresponding author. Mailing address: Department of Pharmacological Sciences, State University of New York at Stony Brook, Stony Brook, NY 11794-8651. Phone: (516) 444-3068. Fax: (516) 444-3218. E-mail: dan{at}pharm.sunysb.edu.

Molecular and Cellular Biology, June 1999, p. 4039-4046, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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