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Submitted on October 9, 2001
Revised on November 19, 2001
Accepted on November 21, 2001

Charting the protein 'complexome' in yeast by mass spectrometry

Raymond J. Deshaies, Jae Hong Seol, Hayes W. McDonald, Greg Cope, Svetlana Lyapina, Andrej Shevchenko, Anna Shevchenko, Rati Verma, and John R. Yates III

Department of Biology, California Institute of Technology, Pasadena, CA 91125

Corresponding Author: deshaies{at}its.caltech.edu

It has become evident over the past few years that many complex cellular processes, including control of the cell cycle and ubiquitin-dependent proteolysis, are carried out by sophisticated multisubunit protein machines that are dynamic in abundance, post-translational modification state, and composition. To understand better the nature of the macromolecular assemblages that carry out the cell cycle and ubiquitin-dependent proteolysis, we have used mass spectrometry extensively over the past few years to characterize both the composition of various protein complexes and the modification states of their subunits. In this article we review some of our recent efforts, and describe a promising new approach for using mass spectrometry to dissect protein interaction networks.


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