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Originally published In Press as doi:10.1074/jbc.M507638200 on September 15, 2005

J. Biol. Chem., Vol. 280, Issue 46, 38657-38665, November 18, 2005
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The 9-1-1 Checkpoint Clamp Physically Interacts with Pol{zeta} and Is Partially Required for Spontaneous Pol{zeta}-dependent Mutagenesis in Saccharomyces cerevisiae*

Simone Sabbioneda{ddagger}1, Brenda K. Minesinger§12, Michele Giannattasio{ddagger}, Paolo Plevani{ddagger}, Marco Muzi-Falconi{ddagger}3, and Sue Jinks-Robertson§¶4

From the {ddagger}Dipartimento di Scienze Biomolecolari e Biotecnologie, Università degli Studi di Milano, Milano, Italy 20133 and the §Biochemistry, Cell and Developmental Biology Program of the Graduate Division of Biological and Biomedical Sciences and the Department of Biology, Emory University, Atlanta, Georgia 30322

The use of translesion synthesis (TLS) polymerases to bypass DNA lesions during replication constitutes an important mechanism to restart blocked/stalled DNA replication forks. Because TLS polymerases generally have low fidelity on undamaged DNA, the cell must regulate the interaction of TLS polymerases with damaged versus undamaged DNA to maintain genome integrity. The Saccharomyces cerevisiae checkpoint proteins Ddc1, Rad17, and Mec3 form a clamp-like structure (the 9-1-1 clamp) that has physical similarity to the homotrimeric sliding clamp proliferating cell nuclear antigen, which interacts with and promotes the processivity of the replicative DNA polymerases. In this work, we demonstrate both an in vivo and in vitro physical interaction between the Mec3 and Ddc1 subunits of the 9-1-1 clamp and the Rev7 subunit of the Pol{zeta} TLS polymerase. In addition, we demonstrate that loss of Mec3, Ddc1, or Rad17 results in a decrease in Pol{zeta}-dependent spontaneous mutagenesis. These results suggest that, in addition to its checkpoint signaling role, the 9-1-1 clamp may physically regulate Pol{zeta}-dependent mutagenesis by controlling the access of Pol{zeta} to damaged DNA.

Received for publication, July 14, 2005 , and in revised form, September 8, 2005.

* This work was supported in part by National Institutes of Health Grant GM064769 (to S. J.-R.), grants from AIRC, Progetto FIRB-MIUR "Genomica e proteomica nello studio di funzioni cellulari complesse," European Union FP6 Integrated Project DNA Repair (to P. P. and M. M.-F.), and Telethon-Italy Grant GGP030406 (to M. M.-F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 Both authors contributed equally to this work.

2 Partially supported by the Graduate Division of Biological and Biomedical Sciences of Emory University.

3 To whom correspondence may be addressed: Via Celoria 26, 20133 Milano, Italy. Tel.: 390250315034; Fax: 390250315044; E-mail: marco.muzifalconi{at}unimi.it. 4 To whom correspondence may be addressed: 1510 Clifton Rd., Atlanta, GA 30322. Tel.: 404-727-6312; Fax: 404-727-2880; E-mail: sue.jinks-robertson{at}emory.edu.


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