Mendoza J A, Horowitz P M
Department of Biochemistry, University of Texas Health Science Center, San Antonio 78240-7760.
J Biol Chem. 1994 Oct 21;269(42):25963-5.
We demonstrate that the previously observed stabilizing effect by the enzyme rhodanese of the oligomeric structure of Cpn60 is general and can be provided by six other proteins that can interact with Cpn60. All these substrate proteins, which include examples that are monomeric, as well as oligomeric polypeptides in their native states, were shown previously to be assisted in their refolding by the chaperonin. Strikingly, during the disassembly of Cpn60 in the presence of any of the substrate proteins, significant amounts of intermediates were detected. Furthermore, unfolded substrate proteins induce the reassembly of tetradecameric Cpn60 from monomers, and binding of each substrate protein stabilizes Cpn60 quaternary structure.
我们证明，先前观察到的硫氰酸酶对Cpn60寡聚体结构的稳定作用具有普遍性，并且可以由其他六种能够与Cpn60相互作用的蛋白质提供。所有这些底物蛋白，包括天然状态下的单体以及寡聚多肽的例子，先前已被证明在伴侣蛋白的帮助下进行重折叠。引人注目的是，在任何底物蛋白存在的情况下，Cpn60解聚过程中检测到大量中间体。此外，未折叠的底物蛋白诱导单体重新组装成十四聚体Cpn60，并且每种底物蛋白的结合都能稳定Cpn60的四级结构。
