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Submitted on July 21, 2005
Revised on September 2, 2005
Accepted on September 9, 2005

Fluorescent proteins as proteomic probes

Ileana M Cristea, Rosemary Williams, Brian T Chait, and Michael P Rout

Rockefeller University, New York

Corresponding Author: rout{at}rockefeller.edu

Protein complexes mediate the majority of cellular processes. Knowledge of the localization and composition of such complexes provides key insights into their functions. Although green fluorescent protein (GFP) has been widely applied for in vivo visualization of proteins, it has been relatively little used as a tool for the isolation of protein complexes. Here, we describe the use of the standard GFP tag to both visualize proteins in living cells and capture their interactions via a simple immunoaffinity purification procedure. We applied this method to the analysis of a variety of endogenous protein complexes from different eukaryotic cells. We show that efficient isolations can be achieved in 5 60 min. This rapid purification helps preserve protein complexes close to their original state in the cell and minimizes non-specific interactions. Given the wide use and availability of GFP-tagged protein reagents, the present method should greatly facilitate the elucidation of many cellular processes.


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