The N-terminus modulates human Caf1 activity, structural stability and aggregation
The N-terminus modulates human Caf1 activity, structural stability and aggregation
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N 末端调节人 Caf1 活性、结构稳定性和聚集
DOI：
10.1016/j.ijbiomac.2012.05.032
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发表时间：
2012-11-01
影响因子：
8.2
通讯作者：
Yan, Yong-Bin
中科院分区：
文献类型：
--
作者：
Feng, Li-Kui;Yan, Yong-Bin
CAF1是CCR4-非复合体中的死烯基酶组分。在这里，我们发现N-末端的去除导致人CAF1(HCaf1)活性下降30%，但对主要结构域结构没有显著影响。N-末端的去掉导致了hCaf1热稳定性的下降，而N-末端的存在促进了hCaf1的热聚集。同源模拟表明，N-末端具有形成与主结构域相互作用的短α-螺旋的能力。因此，N-末端在调节hCaf1的活性、稳定性和聚集性方面发挥了作用。(C)2012爱思唯尔B.V.保留所有权利。
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.