Hsp105 but not Hsp70 family proteins suppress the aggregation of heat‐denatured protein in the presence of ADP

FEBS Letters

Hatayama, Takumi¹  Ishihara, Keiichi¹  Yamagishi, Nobuyuki¹  Saito, Youhei¹ 

[1] Department of Biochemistry, Kyoto Pharmaceutical University, 5 Nakauchi-cho, Misasagi, Yamashina-ku, Kyoto 607-8414, Japan

关键词: Hsp105α;    Hsp105β;    Hsc70;    Thermal aggregation;    ATP;    ADP;    Hsp;    heat shock protein;    CK2;    protein kinase CK2;    PCR;    polymerase chain reaction;    DTT;    dithiothreitol;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;    CBB;    Coomassie brilliant blue;    BSA;    bovine serum albumin;    RCMLA;    reduced carboxymethylated α-lactalbumin;    LA;    α-lactalbumin;   

DOI  :  10.1016/S0014-5793(03)01292-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Hsp105α and Hsp105β are mammalian members of the Hsp105/110 family, a diverged subgroup of the Hsp70 family. Here, we show that Hsp105α and Hsp105β bind non-native protein through the β-sheet domain and suppress the aggregation of heat-denatured protein in the presence of ADP rather than ATP. In contrast, Hsc70/Hsp40 suppressed the aggregation of heat-denatured protein in the presence of ATP rather than ADP. Furthermore, the overexpression of Hsp105α but not Hsp70 in COS-7 cells rescued the inactivation of luciferase caused by ATP depletion. Thus, Hsp105/110 family proteins are suggested to function as a substitute for Hsp70 family proteins to suppress the aggregation of denatured proteins in cells under severe stress, in which the cellular ATP level decreases markedly.

【 授权许可】

Unknown