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Originally published In Press as doi:10.1074/jbc.M201820200 on April 1, 2002

J. Biol. Chem., Vol. 277, Issue 25, 22271-22278, June 21, 2002
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Direct Interaction between Uracil-DNA Glycosylase and a Proliferating Cell Nuclear Antigen Homolog in the Crenarchaeon Pyrobaculum aerophilum*

Hanjing Yang, Ju-Huei Chiang, Sorel Fitz-GibbonDagger , Michel Lebel§, Alessandro A. Sartori, Joseph Jiricny, Malgorzata M. Slupska||, and Jeffrey H. Miller**

From the Department of Microbiology and Molecular Genetics and the Molecular Biology Institute, University of California, Los Angeles, California 90095, § Centre de Recherche en Cancerologie, Pavillon Hotel-Dieu de Quebec, CHUQ Quebec GIR 2J6, Canada, and  Institute of Medical Radiobiology of the University of Zürich and the Paul Scherrer institute, August Forel-Strasse 7, CH-8008 Zürich, Switzerland

Proliferating cell nuclear antigen (PCNA) acts as a sliding clamp on duplex DNA. Its homologs, present in Eukarya and Archaea, are part of protein complexes that are indispensable for DNA replication and DNA repair. In Eukarya, PCNA is known to interact with more than a dozen different proteins, including a human major nuclear uracil-DNA glycosylase (hUNG2) involved in immediate postreplicative repair. In Archaea, only three classes of PCNA-binding proteins have been reported previously: replication factor C (the PCNA clamp loader), family B DNA polymerase, and flap endonuclease. In this study, we report a direct interaction between a uracil-DNA glycosylase (Pa-UDGa) and a PCNA homolog (Pa-PCNA1), both from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum (Topt = 100 °C). We demonstrate that the Pa-UDGa-Pa-PCNA1 complex is thermostable, and two hydrophobic amino acid residues on Pa-UDGa (Phe191 and Leu192) are shown to be crucial for this interaction. It is interesting to note that although Pa-UDGa has homologs throughout the Archaea and bacteria, it does not share significant sequence similarity with hUNG2. Nevertheless, our results raise the possibility that Pa-UDGa may be a functional analog of hUNG2 for PCNA-dependent postreplicative removal of misincorporated uracil.

* This work was supported by National Research Service Award No. T32 CA09056 from the United States Health and Human Services Institutional (to H. Y.), by Grant GM 57917 from the National Institutes of Health (to J. H. M.) and by the generous financial support of the Union Bank of Switzerland Stiftung (to A. A. S).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Center for Astrobiology, Institute of Geophysics and Planetary Physics, UCLA, Los Angeles, CA 90095.

|| Present address: Diversa, 4995 Directors Place, San Diego, CA 92121

** To whom correspondence should be addressed: Dept. of Microbiology and Molecular Genetics, 1602 Molecular Sciences Bldg., 405 Hilgard Ave., Los Angeles, CA 90095. Tel.: 310-825-8460; Fax: 310-206-3088; E-mail: jhmiller@mbi.ucla.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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