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首页> 外文期刊>Nucleic Acids Research >Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing
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Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing

机译：Rcl1p-Bms1p相互作用对酵母核糖体前RNA加工的重要作用

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摘要

The essential Rcl1p and Bms1p proteins form a complex required for 40S ribosomal subunit maturation. Bms1p is a GTPase and Rcl1p has been proposed to catalyse the endonucleolytic cleavage at site A(2) separating the pre-40S and pre-60S maturation pathways. We determined the 2.0 angstrom crystal structure of Bms1p associated with Rcl1p. We demonstrate that Rcl1p nuclear import depends on Bms1p and that the two proteins are loaded into pre-ribosomes at a similar stage of the maturation pathway and remain present within pre-ribosomes after cleavage at A(2). Importantly, GTP binding to Bms1p is not required for the import in the nucleus nor for the incorporation of Rcl1p into pre-ribosomes, but is essential for early pre-rRNA processing. We propose that GTP binding to Bms1p and/or GTP hydrolysis may induce conformational rearrangements within the Bms1p-Rcl1p complex allowing the interaction of Rcl1p with its RNA substrate.
机译：必需的Rcl1p和Bms1p蛋白形成40S核糖体亚基成熟所需的复合物。 Bms1p是一种GTP酶，Rcl1p已被提出来催化位点A（2）的核酸内切裂解，分离了40S之前和60S之前的成熟途径。我们确定与Rcl1p相关的Bms1p的2.0埃晶体结构。我们证明Rcl1p核进口取决于Bms1p，并且这两种蛋白质在成熟途径的相似阶段被加载到核糖体中，并在A（2）裂解后保留在核糖体中。重要的是，GTP与Bms1p的结合对于导入细胞核或将Rcl1p并入核糖体前体而言均不是必需的，但对于早期rRNA的加工至关重要。我们建议GTP绑定到Bms1p和/或GTP水解可能诱导Bms1p-Rcl1p复合体内的构象重排，使Rcl1p与它的RNA底物相互作用。

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