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Molecular and Cellular Biology, September 2002, p. 6480-6486, Vol. 22, No. 18
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.18.6480-6486.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Stimulation of 3'->5' Exonuclease and 3'-Phosphodiesterase Activities of Yeast Apn2 by Proliferating Cell Nuclear Antigen

Ildiko Unk,1 Lajos Haracska,1 Xavier V. Gomes,2 Peter M. J. Burgers,2 Louise Prakash,1 and Satya Prakash1*

Sealy Center for Molecular Science, University of Texas Medical Branch, Galveston, Texas 77555-1061,1 Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 631102

Received 24 April 2002/ Returned for modification 4 June 2002/ Accepted 17 June 2002

The Apn2 protein of Saccharomyces cerevisiae contains 3'->5' exonuclease and 3'-phosphodiesterase activities, and these activities function in the repair of DNA strand breaks that have 3'-damaged termini and which are formed in DNA by the action of oxygen-free radicals. Apn2 also has an AP endonuclease activity and functions in the removal of abasic sites from DNA. Here, we provide evidence for the physical and functional interaction of Apn2 with proliferating cell nuclear antigen (PCNA). As indicated by gel filtration and two-hybrid studies, Apn2 interacts with PCNA both in vitro and in vivo and mutations in the consensus PCNA-binding motif of Apn2 abolish this interaction. Importantly, PCNA stimulates the 3'->5' exonuclease and 3'-phosphodiesterase activities of Apn2. We have examined the involvement of the interdomain connector loop (IDCL) and of the carboxy-terminal domain of PCNA in Apn2 binding and found that Apn2 binds PCNA via distinct domains dependent upon whether the binding is in the absence or presence of DNA. In the absence of DNA, Apn2 binds PCNA through its IDCL domain, whereas in the presence of DNA, when PCNA has been loaded onto the template-primer junction by replication factor C, the C-terminal domain of PCNA mediates the binding.

* Corresponding author. Mailing address: Sealy Center for Molecular Science, University of Texas Medical Branch, 6.104 Medical Research Building, 11th and Mechanic St., Galveston, TX 77555-1061. Phone: (409) 747-8602. Fax: (409) 747-8608. E-mail: s.prakash{at}utmb.edu.

Molecular and Cellular Biology, September 2002, p. 6480-6486, Vol. 22, No. 18
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.18.6480-6486.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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