An active precursor in assembly of yeast nuclear ribonuclease P
An active precursor in assembly of yeast nuclear ribonuclease P
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DOI：
10.1017/s1355838202027048
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发表时间：
2002-10-01
期刊：
影响因子：
4.5
通讯作者：
Engelke, DR
中科院分区：
文献类型：
--
作者：
Srisawat, C;Houser-Scott, F;Engelke, DR
核RNase P的RNA-蛋白质亚基组装通过使用RNA亲和配体特异性分离和表征RNase P的前体和成熟形式来研究。前RNase P在前tRNA切割中与成熟RNase P一样有活性，尽管它只包含在成熟RNase R中发现的9种蛋白中的7种，Pop3 p和Rpr 2 p不是RPR 1 RNA亚基成熟所需的，并且几乎不存在于前RNase P中，这意味着它们是前tRNA底物识别和切割的必需蛋白。RNase P亚基的组装可能发生在核仁中，RNase P RNA的前体和成熟形式都主要位于核仁中。这些结果提供了对核RNase P组装的深入了解，并表明前tRNA底物识别在很大程度上由RNA亚基决定。
The RNA-protein subunit assembly of nuclear RNase P was investigated by specific isolation and characterization of the precursor and mature forms of RNase P using an RNA affinity ligand. Pre-RNase P was as active in pre-tRNA cleavage as mature RNase P, although it contained only seven of the nine proteins found in mature RNase R Pop3p and Rpr2p were not required for maturation of the RPR1 RNA subunit and virtually absent from pre-RNase P, implying that they are dispensable for pre-tRNA substrate recognition and cleavage. The RNase P subunit assembly is likely to occur in the nucleolus, where both precursor and mature forms of RNase P RNA are primarily localized. The results provide insight into assembly of nuclear RNase P, and suggest pre-tRNA substrate recognition is largely determined by the RNA subunit.