Induced folding of the U2AF35 RRM upon binding to U2AF65
Induced folding of the U2AF35 RRM upon binding to U2AF65
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DOI：
10.1016/s0014-5793(02)03294-5
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发表时间：
2002-09-25
期刊：
影响因子：
3.5
通讯作者：
Sattler, M
中科院分区：
文献类型：
--
作者：
Kellenberger, E;Stier, G;Sattler, M
人必需剪接因子U2 AF（U2辅助因子）由35和65 kDa亚基组成，在溶液中形成高度稳定的异源二聚体。重组U2 AF 35 RNA识别基序（U2 AF 35 RRM）和全长U2 AF 65的共纯化产生可溶性和功能活性的最小U2 AF异二聚体。重组U2 AF 35 RRM蛋白游离和与U2 AF 65的三个不同区域的复合物，其特征在于通过核磁共振光谱。我们发现重组U2 AF 35 RRM在溶液中是非结构化的，但其三级结构在与U2 AF 65结合时被诱导。这种相互作用由U2 AF 65的N-末端脯氨酸富集区介导，不涉及U2 AF 65 RRM。(C)2002年欧洲生物化学学会联合会。由Elsevier Science B. V.出版，版权所有。
The human essential splicing factor U2AF (U2 auxiliary factor) consists of 35 and 65 kDa subunits which form a highly stable heterodimer in solution. Copuritication of the recombinant U2AF35 RNA recognition motif (U2AF35 RRM) and full-length U2AF65 yields a soluble and functionally active minimal U2AF heterodimer. Recombinant U2AF35 RRM protein free and in complex with three different regions of U2AF65 was characterized by nuclear magnetic resonance spectroscopy. We found that the recombinant U2AF35 RRM is unstructured in solution but its tertiary structure is induced upon binding to U2AF65. This interaction is mediated by the N-terminal proline-rich region of U2AF65 and does not involve the U2AF65 RRMs. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.