Involvement of the 10-kDa C-terminal fragment of hsc70 in complexing with unfolded protein

被引:28
作者
Hu, SM
Wang, C
机构
[1] ACAD SINICA,INST MOL BIOL,TAIPEI,TAIWAN
[2] NATL DEF MED CTR,GRAD INST LIFE SCI,TAIPEI,TAIWAN
关键词
domains of hsc70; protein complexes; molecular chaperone;
D O I
10.1006/abbi.1996.0328
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Using native gel electrophoresis, we demonstrate that both bovine brain hsc70 and recombinant rat hsc70 form a tightly associated complex with bovine S-carboxymethyl alpha-lactalbumin (CMLA). The formation of the complexes can be inhibited by an octapeptide (KLALSLHD). The recombinant C-terminal 30-kDa fragment also can be tightly associated with CMLA. Consequently, the 44-kDa ATPase domain of hsc70 plays a small role in the formation of the hsc70/CMLA. The N-terminal 60-kDa fragment of hsc70 cannot form a similar complex, despite the finding that the hydrolysis of ATP both by hsc70 and by the 60-kDa fragment can be stimulated by CMLA in a similar concentration-dependent manner with EC(50) values of 15 mu M. Moreover, the C-terminal 10-kDa fragment of hsc70 cannot tightly associate with CMLA, indicating that this fragment is necessary but not sufficient for the formation of the hsc70/CMLA complex. (C) 1996 Academic Press, Inc.
引用
收藏
页码:163 / 169
页数:7
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