HSP60 possesses a GTPase activity and mediates protein folding with HSP10

被引：28
|
作者：
Okamoto, Tomoya [1 ,2 ]
Yamamoto, Hiroshi [1 ,2 ]
Kudo, Ikuru [1 ,2 ]
Matsumoto, Kazuya [3 ,4 ]
Odaka, Masafumi [1 ,2 ]
Grave, Ewa [1 ,2 ]
Itoh, Hideaki [1 ,2 ]
机构：
[1] Akita Univ, Grad Sch, Dept Life Sci, Akita 0108502, Japan
[2] Akita Univ, Fac Engn Sci, Akita 0108502, Japan
[3] Akita Univ, Grad Sch, Dept Appl Chem, Akita 0108502, Japan
[4] Akita Univ, Fac Engn Sci, Akita 0108502, Japan
来源：
SCIENTIFIC REPORTS | 2017年 / 7卷
关键词：
CHAPERONIN GROEL; COOPERATIVITY;
D O I：
10.1038/s41598-017-17167-7
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The mammalian molecular chaperone, HSP60, plays an essential role in protein homeostasis through mediating protein folding and assembly. The structure and ATP-dependent function of HSP60 has been well established in recent studies. After ATP, GTP is the major cellular nucleotide. In this paper, we have investigated the role of GTP in the activity of HSP60. It was found that HSP60 has different properties with respect to allostery, complex formation and protein folding activity depending on the nucleoside triphosphate present. The presence of GTP slightly affected the ATPase activity of HSP60 during protein folding. These results provide clues as to the functional mechanism of the HSP60-HSP10 complex.
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收藏
页数：11
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