Gebauer M, Zeiner M, Gehring U
Institut für Biologische Chemie, Universität Heidelberg, Germany.
FEBS Lett. 1997 Nov 3;417(1):109-13. doi: 10.1016/s0014-5793(97)01267-2.
We investigated several hsp70/hsc70 interacting proteins and established by two independent techniques that hsp40 and Hop/p60 specifically interact with the 257 residue carboxy-terminal domain of hsp70 while Hap-46 and Hip/p48 bind the 383 residue amino-terminal ATP binding domain. Hap-46 and Hip/p48 competed for binding to hsc70, while Hap-46 had no effect on the binding of either Hop/p60 or hsp40 to hsc70. Hap-46 inhibited the refolding of thermally denatured firefly luciferase in an hsc70 and hsp40 dependent assay, and this effect was largely compensated by Hop/p60. These interacting proteins thus appear to cooperate in affecting the chaperoning activity of hsp70/hsc70.
我们研究了几种与hsp70/hsc70相互作用的蛋白质，并通过两种独立技术确定，hsp40和Hop/p60特异性地与hsp70的257个残基羧基末端结构域相互作用，而Hap-46和Hip/p48则结合383个残基的氨基末端ATP结合结构域。Hap-46和Hip/p48竞争与hsc70的结合，而Hap-46对Hop/p60或hsp40与hsc70的结合没有影响。在依赖hsc70和hsp40的检测中，Hap-46抑制了热变性萤火虫荧光素酶的重折叠，而这种作用在很大程度上被Hop/p60所补偿。因此，这些相互作用的蛋白质似乎在影响hsp70/hsc70的伴侣活性方面相互协作。
