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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural and biochemical analysis of the assembly and function of the yeast pre-mRNA 3' end processing complex CF I
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Structural and biochemical analysis of the assembly and function of the yeast pre-mRNA 3' end processing complex CF I

机译：酵母前mRNA 3'末端加工复合物CF I装配和功能的结构和生化分析

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摘要

The accuracy of the 3'-end processing by cleavage and polyadeny-lation is essential for mRNA biogenesis and transcription termination. In yeast, two poorly conserved neighboring elements upstream of cleavage sites are important for accuracy and efficiency of this process. These two RNA sequences are recognized by the RNA binding proteins Hrp1 and Rna 15, but efficient processing in vivo requires a bridging protein (Rna 14), which forms a stable dimer of hetero-dimers with Rna15 to stabilize the RNA-protein complex. We earlier reported the structure of the ternary complex of Rna15 and Hrp1 bound to the RNA processing element. We now report the use of solution NMR to study the interaction of Hrp1 with the Rna14-Rna15 heterodimer in the presence and absence of 3-end processing signals. By using methyl selective labeling on Hrp1, in vivo activity and pull-down assays, we were able to study this complex of several hundred kDa, identify the interface within Hrp1 responsible for recruitment of Rna14 and validate the functional significance of this interaction through structure-driven mutational analysis.
机译：裂解和聚腺苷酸化作用的3'末端加工的准确性对于mRNA生物发生和转录终止至关重要。在酵母中，裂解位点上游两个保守性差的相邻元件对于此过程的准确性和效率很重要。这两个RNA序列可被RNA结合蛋白Hrp1和Rna 15识别，但体内有效加工需要桥接蛋白（Rna 14），该蛋白与Rna15形成稳定的杂二聚体二聚体以稳定RNA蛋白复合物。我们之前报道了与RNA处理元件结合的Rna15和Hrp1三元复合物的结构。我们现在报告使用溶液NMR研究在存在和不存在3末端加工信号的情况下Hrp1与Rna14-Rna15异二聚体的相互作用。通过在Hrp1上使用甲基选择性标记，体内活性和下拉测定法，我们能够研究这种数百kDa的复合物，确定Hrp1内负责招募Rna14的界面，并通过结构验证这种相互作用的功能意义-驱动突变分析。

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