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Molecular & Cellular Proteomics 7:2090-2106, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

A Proteomics Analysis of Yeast Mot1p Protein-Protein Associations

Insights into Mechanism^*,S

Diana R. Arnett, Jennifer L. Jennings, David L. Tabb^¶, Andrew J. Link and P. Anthony Weil^,||

From the Departments of Molecular Physiology and Biophysics and Microbiology and Immunology and the ^¶ Mass Spectrometry Research Center/Departments of Biomedical Informatics and Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0615

Yeast Mot1p, a member of the Snf2 ATPase family of proteins, is a transcriptional regulator that has the unusual ability to both repress and activate mRNA gene transcription. To identify interactions with other proteins that may assist Mot1p in its regulatory processes, Mot1p was purified from replicate yeast cell extracts, and Mot1p-associated proteins were identified by coupled multidimensional liquid chromatography and tandem mass spectrometry. Using this approach we generated a catalog of Mot1p-interacting proteins. Mot1p interacts with a range of transcriptional co-regulators as well as proteins involved in chromatin remodeling. We propose that interaction with such a wide range of proteins may be one mechanism through which Mot1p subserves its roles as a transcriptional activator and repressor.

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