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A more recent version of this article appeared on June 1, 2004
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Submitted on February 4, 2004
Revised on March 11, 2004
Accepted on March 12, 2004
1 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
2 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037; Current address: Department of Genome Sciences, University of Washington, Seattle, WA 91895
3 Department of Cell and Developmental Biology, University of Colorado Health Sciences Center, Denver, CO 80262
* Corresponding author. E-mail address: kathryn.howell{at}uchsc.edu.
The Golgi complex functions to posttranslationally modify newly synthesized proteins and lipids and sort them to their sites of function. In this study, a stacked Golgi fraction was isolated by classical cell fractionation, and the protein complement (the Golgi proteome) was characterized using Multidimensional Protein Identification Technology (MudPIT). Many of the proteins identified are known residents of the Golgi and 64% of these are predicted transmembrane proteins. Proteins localized to other organelles also were identified, strengthening reports of functional interfacing between the Golgi and the endoplasmic reticulum and cytoskeleton. Importantly, 41 proteins of unknown function were identified. Two were selected for further analysis, and Golgi localization was confirmed. One of these, a putative methyltransferase, was shown to be arginine dimethylated, and upon further proteomic analysis, arginine dimethylation was identified on 18 total proteins in the Golgi proteome. This survey illustrates the utility of proteomics in the discovery of novel organellar functions and resulted in: 1) a protein profile of an enriched Golgi fraction, 2) identification of 41 previously uncharacterized proteins, two with confirmed Golgi localization, 3) the identification of arginine dimethylated residues in Golgi proteins, and 4) a confirmation of methyltransferase activity within the Golgi fraction.
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