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J. Biol. Chem., Vol. 282, Issue 5, 2976-2986, February 2, 2007

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Characterization of the Interactome of the Human MutL Homologues MLH1, PMS1, and PMS2^*

Elda Cannavo, Bertran Gerrits, Giancarlo Marra, Ralph Schlapbach, and Josef Jiricny¹

From the Institute of Molecular Cancer Research and the Functional Genomics Center Zurich, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland

Postreplicative mismatch repair (MMR) involves the concerted action of at least 20 polypeptides. Although the minimal human MMR system has recently been reconstituted in vitro, genetic evidence from different eukaryotic organisms suggests that some steps of the MMR process may be carried out by more than one protein. Moreover, MMR proteins are involved also in other pathways of DNA metabolism, but their exact role in these processes is unknown. In an attempt to gain novel insights into the function of MMR proteins in human cells, we searched for interacting partners of the MutL homologues MLH1 and PMS2 by tandem affinity purification and of PMS1 by large scale immunoprecipitation. In addition to proteins known to interact with the MutL homologues during MMR, mass spectrometric analyses identified a number of other polypeptides, some of which bound to the above proteins with very high affinity. Whereas some of these interactors may represent novel members of the mismatch repairosome, others appear to implicate the MutL homologues in biological processes ranging from intracellular transport through cell signaling to cell morphology, recombination, and ubiquitylation.

Received for publication, October 24, 2006 , and in revised form, December 4, 2006.

^* This work was supported in part by grants from the Swiss National Science Foundation, the European Union, and the Bonizzi-Theler Stiftung (to J. J.). 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 To whom correspondence should be addressed: Institute of Molecular Cancer Research, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland. Tel.: 41-44-6353450; Fax: 41-44-6353484; E-mail: jiricny{at}imcr.unizh.ch.

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