表面诱导解离产生20S蛋白酶体复合物的亚结构。
Surface induced dissociation yields substructure of 20S proteasome complexes.
作者信息
Ma Xin, Loo Joseph A, Wysocki Vicki H
机构信息
Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.
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.
出版信息
Int J Mass Spectrom. 2015 Feb 1;377:201-204. doi: 10.1016/j.ijms.2014.09.011.
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, 20S proteasome, which consists of four stacked heptameric rings (αββα 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 αβ fragment, 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.
摘要
原生质谱（MS）和表面诱导解离（SID）已被应用于研究非共价蛋白质复合物的化学计量和四级结构。在本研究中，由四个堆叠的七聚体环（αββα对称性）组成的20S蛋白酶体被选来探索复杂堆叠环蛋白质复合物的SID解离模式。SID产生α和β亚基，而碰撞诱导解离（CID）仅产生高电荷的α亚基。此外，电荷减少的20S蛋白酶体产生αβ片段，反映了复合物的堆叠环拓扑结构。结果表明，SID和电荷减少的结合是研究蛋白质复合物结构的有力工具。
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