The N-terminus modulates human Caf1 activity, structural stability and aggregation

被引：3
|
作者：
Feng, Li-Kui [1 ]
Yan, Yong-Bin [1 ]
机构：
[1] Tsinghua Univ, Sch Life Sci, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China
来源：
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2012年 / 51卷 / 04期
基金：
中国国家自然科学基金;
关键词：
Aggregation kinetics; Homology modeling; Thermal stability; MESSENGER-RNA DEADENYLASE; SEQUENTIAL EVENTS; PROTEIN; ROLES; YEAST; SUPPRESSION; SUBUNIT; REGIONS; COMPLEX; PLAYS;
D O I：
10.1016/j.ijbiomac.2012.05.032
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：
Caf1 is a deadenylase component of the CCR4-Not complex. Here we found that the removal of the N-terminus resulted in a 30% decrease in human Caf1 (hCaf1) activity, but had no significant influence on main domain structure. The removal of the N-terminus led to a decrease in the thermal stability, while the existence of the N-terminus promoted hCaf1 thermal aggregation. Homology modeling indicated that the N-terminus had a potency to form a short alpha-helix interacted with the main domain. Thus the N-terminus played a role in modulating hCaf1 activity, stability and aggregation. (C) 2012 Elsevier B.V. All rights reserved.
引用
收藏
页码：497 / 503
页数：7
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