Study on assembly mechanism of 20S proteasome through the structural analysis of its intermediates
The 20S proteasome plays a main role, degrading unnecessary proteins, in a protein-metabolic system. This large protein has a hollow cylindrical shape consisting of four rings, a, b, b, a. Both a- and b-rings are heptamers with a1-a7 subunits and b1-b7 ones, respectively. This means that 28 subunits should be timely and precisely arranged to form the active 20S proteasome. It is considered that there are three steps to fabricate the 20S proteasome: the first step is formation of a single a-ring, and the second step is formation of a half proteasome by conjugation of b1-b7 subunits to the single a-ring, and the third step is connection of two half proteasomes. The aim of this study is to reveal the assembly mechanism of a1-a7 subunits in the first step through the clarification of the structure of the intermediates. We have already found several candidates of the intermediates, which are assemblies with a-subunit(s) and chaperones. Because the assemblies have not been crystallized, we will determine the configurations of subunits in the assemblies with small-angle neutron scattering by utilizing contrast matching technique of 75% deuterated protein in 100% D2O solvent.
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Masaaki Sugiyama; INOUE Rintaro; MARTEL Anne; PORCAR Lionel; VIGILD Martin; YAGI Hirokazu and ZACCAI Joseph. (2016). Study on assembly mechanism of 20S proteasome through the structural analysis of its intermediates. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-884
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