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Originally published In Press as doi:10.1074/mcp.M200030-MCP200 on July 26, 2002.
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Molecular & Cellular Proteomics 1:567-578, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Mapping and Structural Dissection of Human 20 S Proteasome Using Proteomic Approaches*

Stephane Claverol, Odile Burlet-Schiltz, Elisabeth Girbal-Neuhauser, Jean Edouard Gairin and Bernard Monsarrat{ddagger}

From the Institut de Pharmacologie et de Biologie Structurale, CNRS, 205 Route de Narbonne, 31077 Toulouse, France

{ddagger} To whom correspondence should be addressed: Institut de Pharmacologie et de Biologie Structurale, CNRS UMR 5089, 205 Route de Narbonne, 31077 Toulouse, France. Tel.: 33-5-61-17-55-45; Fax: 33-5-61-17-55-49; E-mail: Bernard.Monsarrat{at}ipbs.fr

The proteasome, a proteolytic complex present in all eukaryotic cells, is part of the ATP-dependent ubiquitin/proteasome pathway. It plays a critical role in the regulation of many physiological processes. The 20 S proteasome, the catalytic core of the 26 S proteasome, is made of four stacked rings of seven subunits each ({alpha}7ß7ß7{alpha}7). Here we studied the human 20 S proteasome using proteomics. This led to the establishment of a fine subunit reference map and to the identification of post-translational modifications. We found that the human 20 S proteasome, purified from erythrocytes, exhibited a high degree of structural heterogeneity, characterized by the presence of multiple isoforms for most of the {alpha} and ß subunits, including the catalytic ones, resulting in a total of at least 32 visible spots after Coomassie Blue staining. The different isoforms of a given subunit displayed shifted pI values, suggesting that they likely resulted from post-translational modifications. We then took advantage of the efficiency of complementary mass spectrometric approaches to investigate further these protein modifications at the structural level. In particular, we focused our efforts on the {alpha}7 subunit and characterized its N-acetylation and its phosphorylation site localized on Ser250.


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