Johnston S C, Whitby F G, Realini C, Rechsteiner M, Hill C P
Biochemistry Department, University of Utah, Salt Lake City 84132, USA.
Protein Sci. 1997 Nov;6(11):2469-73. doi: 10.1002/pro.5560061123.
Activity of the 20S proteasome, which performs much of the cytosolic and nuclear proteolysis in eukaryotic cells, is controlled by regulatory complexes that bind to one or both ends of the cylindrical proteasome. One of these complexes, the 11S regulator (REG), is a complex of 28 kDa subunits that is thought to activate proteasomes toward the production of antigenic peptides. REG, purified from red blood cells, is a complex of REG alpha and REG beta subunits. We have crystallized recombinant REG alpha (rREG alpha) and collected diffraction data to 3.0 A resolution. The self-rotation function indicates that rREG alpha forms a heptameric ring in the crystal. Equilibrium sedimentation demonstrates that rREG alpha is a heptamer in solution also.
20S蛋白酶体在真核细胞中承担着大部分胞质和核内的蛋白质水解活动,其活性受与圆柱形蛋白酶体一端或两端结合的调节复合物控制。其中一种复合物,即11S调节因子(REG),是由28 kDa亚基组成的复合物,被认为能激活蛋白酶体以产生抗原肽。从红细胞中纯化得到的REG是REGα和REGβ亚基的复合物。我们已使重组REGα(rREGα)结晶,并收集到了分辨率为3.0 Å的衍射数据。自旋转函数表明rREGα在晶体中形成七聚体环。平衡沉降实验表明rREGα在溶液中也是七聚体。