INTERACTION OF HSP70 WITH UNFOLDED PROTEINS - EFFECTS OF TEMPERATURE AND NUCLEOTIDES ON THE KINETICS OF BINDING

被引：329

作者：

PALLEROS, DR

WELCH, WJ

FINK, AL

机构：

[1] UNIV CALIF SANTA CRUZ,DEPT CHEM & BIOCHEM,SANTA CRUZ,CA 95064

[2] UNIV CALIF SAN FRANCISCO,DEPT MED,SAN FRANCISCO,CA 94143

[3] UNIV CALIF SAN FRANCISCO,DEPT PHYSIOL,SAN FRANCISCO,CA 94143

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 13期

关键词：

HEAT SHOCK PROTEINS; THERMAL STABILITY; NUCLEOTIDE BINDING;

D O I：

10.1073/pnas.88.13.5719

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：

Circular dichroism and HPLC gel filtration were used to show that cytosolic hsp70 is thermally stable but undergoes a conformational transition (midpoint, 43-degrees-C; 57-degrees-C in the presence of ATP or ADP) leading to oligomerization. hsp70 binds to unfolded, but not to folded, proteins in a temperature-dependent manner; complex formation is significant only at physiologically relevant temperatures. hsp70 binds ADP more tightly than ATP to form a binary complex, which binds to the unfolded protein more rapidly than free hsp70. ADP also inhibits the ATP-induced dissociation of the hsp70-protein complex. A regulatory role for the hsp70-nucleotide binary complexes is proposed.

引用

页码：5719 / 5723

页数：5

共 22 条

[1] INTERACTION OF HSP-70 WITH NEWLY SYNTHESIZED PROTEINS - IMPLICATIONS FOR PROTEIN FOLDING AND ASSEMBLY [J].