Exploring the Functional Complementation between Grp94 and Hsp90.
Exploring the Functional Complementation between Grp94 and Hsp90.
复制标题
DOI：
10.1371/journal.pone.0166271
复制
发表时间：
2016
期刊：
影响因子：
3.7
通讯作者：
Gewirth DT
中科院分区：
文献类型：
--
作者：
Maharaj KA;Que NL;Hong F;Huck JD;Gill SK;Wu S;Li Z;Gewirth DT
Grp94 and Hsp90 are the ER and cytoplasmic paralog members, respectively, of the hsp90 family of molecular chaperones. The structural and biochemical differences between Hsp90 and Grp94 that allow each paralog to efficiently chaperone its particular set of clients are poorly understood. The two paralogs exhibit a high degree of sequence similarity, yet also display significant differences in their quaternary conformations and ATPase activity. In order to identify the structural elements that distinguish Grp94 from Hsp90, we characterized the similarities and differences between the two proteins by testing the ability of Hsp90/Grp94 chimeras to functionally substitute for the wild-type chaperones in vivo. We show that the N-terminal domain or the combination of the second lobe of the Middle domain plus the C-terminal domain of Grp94 can functionally substitute for their yeast Hsp90 counterparts but that the equivalent Hsp90 domains cannot functionally replace their counterparts in Grp94. These results also identify the interface between the Middle and C-terminal domains as an important structural unit within the Hsp90 family.
登录
查看更多内容
影响因子：
16.6
作者：
Liu, Bei;Yang, Yi;Qiu, Zhijuan;Staron, Matthew;Hong, Feng;Li, Yi;Wu, Shuang;Li, Yunfeng;Hao, Bing;Bona, Robert;Han, David;Li, Zihai
通讯作者：
Li, Zihai
影响因子：
5.6
作者：
Immormino, Robert M.;Metzger, Louis E.;Reardon, Patrick N.;Dollins, D. Eric;Blagg, Brian S. J.;Gewirth, Daniel T.
通讯作者：
Gewirth, Daniel T.
影响因子：
4.8
作者：
Dollins, DE;Immormino, RM;Gewirth, DT
通讯作者：
Gewirth, DT
影响因子：
5.7
作者：
Harris, SF;Shiau, AK;Agard, DA
通讯作者：
Agard, DA
DOI：
10.1016/j.bbamcr.2011.08.013
发表时间：
2012-03
期刊：
Biochimica et biophysica acta
影响因子：
--
作者：
Hartson SD;Matts RL
通讯作者：
Matts RL