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Submitted on May 24, 2002
Institut de Pharmacologie et de Biologie Structurale, CNRS, Toulouse 31077
Corresponding Author: 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 20S proteasome, the catalytic core of the 26S proteasome, is made of four stacked rings of 7 subunits each (
Revised on July 26, 2002
Accepted on July 26, 2002
Mapping and Structural Dissection of Human 20S Proteasome using Proteomics Approaches
7
777). Here we studied the human 20S 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 20S proteasome, purified from erythrocytes, exhibited a high degree of structural heterogeneity, characterized by the presence of multiple isoforms for most of the and 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 pIs, 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 7 subunit and characterized its N-acetylation and its phosphorylation site localized on Ser250
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