Length of polyglutamine tract affects secondary and tertiary structures of huntingtin protein

被引：6

作者：

Vachharajani, Shivang N. ^{[1
]}

Chaudhary, Rajeev Kumar ^{[1
]}

Prasad, Shivcharan ^{[1
]}

Roy, Ipsita ^{[1
]}

机构：

[1] Natl Inst Pharmaceut Educ & Res NIPER, Dept Biotechnol, Sas Nagar 160062, Punjab, India

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2012年 / 51卷 / 05期

关键词：

Chaotrope; Huntingtin; Huntington's disease; Polyglutamine; Protein stability; EXPANSION; ATAXIN-3; DISEASE; AGGREGATION; EXPRESSION; FIBRILS; DEATH;

D O I：

10.1016/j.ijbiomac.2012.07.022

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：

The role of polyglutamine (polyQ) tract on protein stability and disease pathology remains ambiguous. We monitored the unfolding/refolding patterns of huntingtin proteins with varying polyQ lengths. In the presence of urea, minor differences in unfolding and refolding efficiencies were observed. However, in the presence of guanidinium hydrochloride, the protein with a longer polyQ stretch was able to regain its secondary but not tertiary structure on step-wise removal of denaturant. Thus, in case of Huntington's disease, the higher aggregation propensity of the mutant protein is likely to be due to the lower stability of the protein due to elongated polyQ tract. (C) 2012 Elsevier B.V. All rights reserved.

引用

页码：920 / 925

页数：6

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