title: Surface induced dissociation yields substructure ofMethanosarcina thermophila20S 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 thermophila20S proteasome, which consists of four stacked heptameric rings (α7β7β7α7symmetry), 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 α7β7fragment, reflecting the stacked ring topology of the complex. The combination of SID and charge reduction is shown to be a powerful tool for the study of protein complex structure.
authors.affiliation: Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.
authors.forename: Xin
authors.initials: X
authors.lastname: Ma
authors.affiliation: Department of Biological Chemistry, Department of Chemistry & Biochemistry, and UCLA/DOE Institute for Genomics and Proteomics, University of California, Los Angeles, Los Angeles, California 90095, United States.
authors.forename: Joseph A
authors.initials: JA
authors.lastname: Loo
authors.affiliation: Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.
authors.forename: Vicki H
authors.initials: VH
authors.lastname: Wysocki
keywords: 20S proteasome; charge reduction; native mass spectrometry; stacked ring; surface induced dissociation; triethylammonium acetate