Conformational lability of two molecular chaperones Hsc70 and gp96: Effects of pH and temperature

被引：20

作者：

Fan, HH

Kashi, RS

Middaugh, CR ^{[1
]}

机构：

[1] Univ Kansas, Dept Pharmaceut Chem, Lawrence, KS 66047 USA

[2] Antigen Inc, Lexington, MA 02421 USA

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2006年 / 447卷 / 01期

关键词：

heat shock protein; Hsc70; gp96; conformational lability; empirical phase diagram;

D O I：

10.1016/j.abb.2006.01.012

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：

Hsc70 and gp96 are two heat shock proteins with molecular chaperone and immune-related activities. The dynamic conformational properties of heat shock proteins appear to play a critical role in their biological activities. In this study, we investigated the effects of pH and temperature on the conformational states of Hsc70 and gp96. The quaternary, tertiary, and secondary structures of both proteins are evaluated by a variety of spectroscopic techniques, including far-UV circular dichroism, Trp fluorescence, ANS fluorescence, and derivative UV absorption spectroscopy. The results are summarized and compared employing an empirical phase diagram approach. Very similar behaviors are seen for both proteins despite their differences in sequence and tertiary structure. Both proteins show substantial conformational lability in responses to the pH and temperature changes of their environment. This study suggests a natural selection for related functional properties through common conformational dynamics rather than immediate structural homology. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：34 / 45

页数：12

共 40 条

[1] Aggregation of hsp70 and hsc70 in vivo is distinct and temperature-dependent and their chaperone function is directly related to non-aggregated forms [J].