The C-terminal WD40 repeats on the TOPLESS co-repressor function as a protein-protein interaction surface
The C-terminal WD40 repeats on the TOPLESS co-repressor function as a protein-protein interaction surface
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DOI：
10.1007/s11103-019-00842-w
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发表时间：
2019-05-01
影响因子：
5.1
通讯作者：
Gurley, William
中科院分区：
文献类型：
--
作者：
Collins, Joe;O'Grady, Kevin;Gurley, William
关键信息TOPLESS上的两个预测的WD 40螺旋桨作为蛋白质-蛋白质相互作用结构域发挥作用。第一个WD 40螺旋桨介导与RAV 1的相互作用，第二个WD 40螺旋桨介导与VRN 5的相互作用。通过这些相互作用，TPL/TPR在越来越多样化的植物途径中抑制转录。结合TPL/TPR的蛋白质通常含有一个或多个介导相互作用的抑制结构域（RD）。例如，已知充分表征的乙烯反应因子相关的两亲性阻遏（Amphiphilic Representation，缩写为ERF）基序通过结合位于N-末端的TOPLESS结构域（TPD）来促进相互作用。在这里，我们表明，在酵母双杂交试验中，与ABI 3/VP 1 -1（RAV 1）相关的非-cDNA 3蛋白结合位于TPL的前9个WD 40重复序列内的新区域。蛋白质建模和计算机模拟分析表明，这九个WD 40重复序列可能形成位于TPL C-末端的两个WD 40螺旋桨中的第一个。RAV 1和第一个WD 40螺旋桨之间的相互作用与另一个RAV家族成员TEMPRANILLO 1（TEM 1）是保守的，并由位于RAV 1和TEM 1上的B3抑制结构域（BRD）介导。此外，预测的第二个WD 40推进器在酵母细胞中显示结合春化5（VRN 5），其中包含几个未经证实的部分RD。此外，我们证明了TPL的第一个WD 40推进器可以在酵母和拟南芥原生质体中与RAV 1形成复合物。
Key messageThe two predicted WD40 propellers on TOPLESS function as protein-protein interaction domains. The 1st WD40 propeller mediates interaction with RAV1, and the 2nd WD40 propeller mediates interaction with VRN5.AbstractThe TOPLESS/TOPLESS-RELATED (TPL/TPR) co-repressor family proteins are known to interact with a wide variety of proteins including transcription factors, Mediator subunits, histone deacetylases, and histone tails. Through these interactions, TPL/TPR act to repress transcription in an increasingly diverse array of plant pathways. Proteins that bind TPL/TPR typically contain one or more Repression Domains (RDs) that mediate the interaction. For example, the well-characterized Ethylene response factor-associated Amphiphilic Repression (EAR) motif is known to facilitate interaction by binding the TOPLESS Domain (TPD) located in the N-terminus. Here we show that in yeast two-hybrid assays, the non-EAR protein, Related to ABI3/VP1-1 (RAV1), binds a novel region located within the first nine WD40-repeats of TPL. Protein modeling and in silico analysis suggest that these nine WD40 repeats may form the first of two WD40 propellers located on C-terminus of TPL. The interaction between RAV1 and the 1st WD40 propeller is conserved with another RAV family member, TEMPRANILLO1 (TEM1) and is mediated by the B3 Repression Domain (BRD) located on both RAV1 and TEM1. Also, the predicted 2nd WD40 propeller was shown in yeast cells to bind Vernalization 5 (VRN5), which contains several unconfirmed partial RDs. Furthermore, we demonstrate that the 1st WD40 propeller of TPL can form a complex with RAV1 both in yeast and in Arabidopsis protoplasts.