Surface induced dissociation yields substructure of Methanosarcina thermophila 20S proteasome complexes.

ABSTRACT: Native mass spectrometry (MS) and surface induced dissociation (SID) have been applied to study the stoichiometry and quaternary structure of non-covalent protein complexes. In this study, Methanosarcina thermophila 20S proteasome, which consists of four stacked heptameric rings (α₇β₇β₇α₇ symmetry), has been selected to explore the SID dissociation pattern of a complicated stacked ring protein complex. SID produces both α and β subunits while collision induced dissociation (CID) produces only highly charged α subunit. In addition, the charge reduced 20S proteasome produces the α₇β₇ fragment, reflecting the stacked ring topology of the complex. The combination of SID and charge reduction is shown to be a powerful tool

SUBMITTER: Ma X 

PROVIDER: S-EPMC4441206 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature