异质性核糖核蛋白A1（hnRNP A1）紧密相关的串联RNA识别基序的不同功能。
Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1.
作者信息
Mayeda A, Munroe S H, Xu R M, Krainer A R
机构信息
Cold Spring Harbor Laboratory, New York 11724-2208, USA.
出版信息
RNA. 1998 Sep;4(9):1111-23. doi: 10.1017/s135583829898089x.
Abstract
hnRNP A1 regulates alternative splicing by antagonizing SR proteins. It consists of two closely related, tandem RNA-recognition motifs (RRMs), followed by a glycine-rich domain. Analysis of variant proteins with duplications, deletions, or swaps of the RRMs showed that although both RRMs are required for alternative splicing function, each RRM plays distinct roles, and their relative position is important. Surprisingly, RRM2 but not RRM1 could support this function when duplicated, despite their very similar structure. Specific RNA binding and annealing are not sufficient for hnRNP A1 alternative splicing function. These observations, together with phylogenetic and structural data, suggest that the two RRMs are quasi-symmetric but functionally nonequivalent modules that evolved as components of a single bipartite domain.
摘要
异质性核糖核蛋白A1（hnRNP A1）通过拮抗丝氨酸/精氨酸丰富蛋白（SR蛋白）来调节可变剪接。它由两个紧密相关的串联RNA识别基序（RRMs）组成，后面跟着一个富含甘氨酸的结构域。对RRMs重复、缺失或交换的变异蛋白的分析表明，虽然两个RRMs都是可变剪接功能所必需的，但每个RRMs发挥着不同的作用，并且它们的相对位置很重要。令人惊讶的是，尽管RRM2和RRM1结构非常相似，但只有RRM2在重复时能够支持这种功能。特异性RNA结合和退火不足以实现hnRNP A1的可变剪接功能。这些观察结果，连同系统发育和结构数据表明，两个RRMs是准对称但功能不等价的模块，它们作为单个二分结构域的组成部分进化而来。
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