一种包含 U6 RNA 片段的复合物的结构和功能意义，该片段由 Prp24 的一个结构域结合。
Structure and functional implications of a complex containing a segment of U6 RNA bound by a domain of Prp24.
机构信息
Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
出版信息
RNA. 2010 Apr;16(4):792-804. doi: 10.1261/rna.1913310. Epub 2010 Feb 24.
Abstract
U6 RNA plays a critical role in pre-mRNA splicing. Assembly of U6 into the spliceosome requires a significant structural rearrangement and base-pairing with U4 RNA. In the yeast Saccharomyces cerevisiae, this process requires the essential splicing factor Prp24. We present the characterization and structure of a complex containing one of Prp24's four RNA recognition motif (RRM) domains, RRM2, and a fragment of U6 RNA. NMR methods were used to identify the preferred U6 binding sequence of RRM2 (5'-GAGA-3'), measure the affinity of the interaction, and solve the structure of RRM2 bound to the hexaribonucleotide AGAGAU. Interdomain contacts observed between RRM2 and RRM3 in a crystal structure of the free protein are not detectable in solution. A structural model of RRM1 and RRM2 bound to a longer segment of U6 RNA is presented, and a partial mechanism for Prp24's annealing activity is proposed.
摘要
U6 RNA 在 pre-mRNA 剪接中起着关键作用。U6 与 U4 RNA 形成剪接体需要进行重大的结构重排和碱基配对。在酵母酿酒酵母中，这一过程需要必需的剪接因子 Prp24。我们介绍了一个包含 Prp24 的四个 RNA 识别基序（RRM）结构域之一的 RRM2 和 U6 RNA 片段的复合物的特征和结构。NMR 方法用于鉴定 RRM2 的 U6 结合序列（5'-GAGA-3'），测量相互作用的亲和力，并解析 RRM2 与六聚核苷酸 AGAGAU 结合的结构。在游离蛋白的晶体结构中观察到的 RRM2 和 RRM3 之间的结构域间接触在溶液中无法检测到。提出了 RRM1 和 RRM2 与 U6 RNA 较长片段结合的结构模型，并提出了 Prp24 退火活性的部分机制。
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