Deciphering preferential interactions within supramolecular protein complexes: the proteasome case.

ABSTRACT: In eukaryotic cells, intracellular protein breakdown is mainly performed by the ubiquitin-proteasome system. Proteasomes are supramolecular protein complexes formed by the association of multiple sub-complexes and interacting proteins. Therefore, they exhibit a very high heterogeneity whose function is still not well understood. Here, using a newly developed method based on the combination of affinity purification and protein correlation profiling associated with high-resolution mass spectrometry, we comprehensively characterized proteasome heterogeneity and identified previously unknown preferential associations within proteasome sub-complexes. In particular, we showed for the first time that the two main proteasome subtypes, standard proteasome and immunoproteasome, interact with a diffe

SUBMITTER: Fabre B 

PROVIDER: S-EPMC4332148 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature