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Published online 1 June 2004

Nucleic Acids Research, 2004, Vol. 32, No. 10 3005-3016
© 2004 Oxford University Press

The C-terminal zinc finger of the catalytic subunit of DNA polymerase {delta} is responsible for direct interaction with the B-subunit

Javier Sanchez Garcia, Leonora F. Ciufo, Xiaowen Yang1, Stephen E. Kearsey1 and Stuart A. MacNeill*

Wellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, King’s Buildings, Mayfield Road, Edinburgh EH9 3JR, UK and 1 Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, UK

*To whom correspondence should be addressed: Tel: +44 131 650 7088; Fax: +44 131 650 5379; Email: s.a.macneill{at}ed.ac.uk
Present address:
Leonora F. Cuifo, Department of Physiology, University of Liverpool, Crown Street, Liverpool L69 3BX, UK

Received April 2, 2004; Revised and Accepted May 6, 2004

DNA polymerase {delta} (Pol {delta}) plays a central role in eukaryotic chromosomal DNA replication, repair and recombination. In fission yeast, Pol {delta} is a tetrameric enzyme, comprising the catalytic subunit Pol3 and three smaller subunits, Cdc1, Cdc27 and Cdm1. Previous studies have demonstrated a direct interaction between Pol3 and Cdc1, the B-subunit of the complex. Here it is shown that removal of the tandem zinc finger modules located at the C-terminus of Pol3 by targeted proteolysis renders the Pol3 protein non-functional in vivo, and that the C-terminal zinc finger module ZnF2 is both necessary and sufficient for binding to the B-subunit in vivo and in vitro. Extensive mutagenesis of the ZnF2 module identifies important residues for B-subunit binding. In particular, disruption of the ZnF2 module by substitution of the putative metal-coordinating cysteines with alanine abolishes B-subunit binding and in vivo function. Finally, evidence is presented suggesting that the ZnF region is post-translationally modified in fission yeast cells.


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