A Proteomics Analysis of Yeast Mot1p Protein-Protein Associations INSIGHTS INTO MECHANISM

被引：14

作者：

Arnett, Diana R. ^{[1
]}

Jennings, Jennifer L. ^{[2
]}

Tabb, David L. ^{[3
,4
]}

Link, Andrew J. ^{[2
]}

Weil, P. Anthony ^{[1
]}

机构：

[1] Vanderbilt Univ, Sch Med, Dept Mol Physiol & Biophys, Nashville, TN 37232 USA

[2] Vanderbilt Univ, Sch Med, Dept Microbiol & Immunol, Nashville, TN 37232 USA

[3] Vanderbilt Univ, Sch Med, Mass Spectrometry Res Ctr, Dept Biomed Informat, Nashville, TN 37232 USA

[4] Vanderbilt Univ, Sch Med, Mass Spectrometry Res Ctr, Dept Biochem, Nashville, TN 37232 USA

来源：

MOLECULAR & CELLULAR PROTEOMICS | 2008年 / 7卷 / 11期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1074/mcp.M800221-MCP200

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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. Molecular & Cellular Proteomics 7: 2090-2106, 2008.

引用

页码：2090 / 2106

页数：17

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