核糖核蛋白核糖核酸酶 MRP 的底物识别。
Substrate recognition by ribonucleoprotein ribonuclease MRP.
机构信息
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
出版信息
RNA. 2011 Feb;17(2):356-64. doi: 10.1261/rna.2393711. Epub 2010 Dec 20.
Abstract
The ribonucleoprotein complex ribonuclease (RNase) MRP is a site-specific endoribonuclease essential for the survival of the eukaryotic cell. RNase MRP closely resembles RNase P (a universal endoribonuclease responsible for the maturation of the 5' ends of tRNA) but recognizes distinct substrates including pre-rRNA and mRNA. Here we report the results of an in vitro selection of Saccharomyces cerevisiae RNase MRP substrates starting from a pool of random sequences. The results indicate that RNase MRP cleaves single-stranded RNA and is sensitive to sequences in the immediate vicinity of the cleavage site requiring a cytosine at the position +4 relative to the cleavage site. Structural implications of the differences in substrate recognition by RNases P and MRP are discussed.
摘要
核糖核蛋白复合物核糖核酸酶（RNase）MRP 是一种具有细胞生存必需的、位点特异性的内切核糖核酸酶。RNase MRP 非常类似于 RNase P（一种负责 tRNA 5'端成熟的普遍内切核糖核酸酶），但能识别不同的底物，包括前 rRNA 和 mRNA。在此，我们报告了从随机序列池中体外选择酿酒酵母 RNase MRP 底物的结果。结果表明，RNase MRP 可切割单链 RNA，并且对切割位点附近的序列敏感，需要在切割位点后第 +4 位有一个胞嘧啶。RNase P 和 MRP 底物识别差异的结构影响也进行了讨论。
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