Weird fingers: Functional analysis of WIP domain proteins
Weird fingers: Functional analysis of WIP domain proteins
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DOI：
10.1016/j.febslet.2010.06.007
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发表时间：
2010-07-16
期刊：
影响因子：
3.5
通讯作者：
Sagasser, Martin
中科院分区：
文献类型：
--
作者：
Appelhagen, Ingo;Huep, Gunnar;Sagasser, Martin
C2 H2锌指蛋白是一种植物特异性的锌指蛋白亚家族。在这项研究中，我们的功能特点的蛋白质结构域，其中包括四个ZF基序，并讨论蛋白质的分子功能。每个ZF中的突变导致拟南芥中TT 1/WIP 1蛋白的功能丧失。在两个ZF中检测到SV 40型核定位信号，并使用GFP融合以及通过TILLING鉴定的新突变等位基因进行功能表征。启动子交换实验表明，选定的TT 1蛋白能够部分接管TT 1功能。通过向TT 2-TT 8-TTG 1调节复合物中添加TT 1，可以增加AtBAN启动子（潜在的TT 1靶标）的活性。(C)2010年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
WIP proteins form a plant specific subfamily of C2H2 zinc finger (ZF) proteins. In this study, we functionally characterized the WIP domain, which consists of four ZF motifs, and discuss molecular functions for WIP proteins. Mutations in each of the ZFs lead to loss of function of the TT1/WIP1 protein in Arabiopsis thaliana. SV40 type nuclear localisation signals were detected in two of the ZFs and functionally characterized using GFP fusions as well as new mutant alleles identified by TILLING. Promoter swap experiments showed that selected WIP proteins are partially able to take over TT1 function. Activity of the AtBAN promoter, a potential TT1 target, could be increased by the addition of TT1 to the TT2-TT8-TTG1 regulatory complex. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.