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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Genome-wide search for yeast RNase P substrates reveals role in maturation of intron-encoded box C/D small nucleolar RNAs
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Genome-wide search for yeast RNase P substrates reveals role in maturation of intron-encoded box C/D small nucleolar RNAs

机译：全基因组搜索酵母RNase P底物揭示了内含子编码盒C / D小核仁RNA成熟的作用

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摘要

Ribonuclease P (RNase P) is an essential endonuclease responsible for the 5'-end maturation of precursor tRNAs. Bacterial RNase P also processes precursor 4.5S RNA, tmRNA, 30S preribosomal RNA, and several reported protein-coding RNAs. Eukaryotic nuclear RNase P is far more complex than in the bacterial form, employing multiple essential protein subunits in addition to the catalytic RNA subunit. RNomic studies have shown that RNase P binds other RNAs in addition to tRNAs, but no non-tRNA substrates have previously been identified. Additional substrates were identified by using a multipronged approach in the budding yeast Saccha-romyces cerevisiae. First, RNase P-dependant changes in RNA abundance were examined on whole-genome microarrays by using strains containing temperature sensitive (TS) mutations in two of the essential RNase P subunits, Pop1p and Rpr1r. Second, RNase P was rapidly affinity-purified, and copurif ied RNAs were identified by using a genome-wide microarray. Third, to identify RNAs that do not change abundance when RNase P is depleted but accumulate as larger precursors, >80 potential small RNA substrates were probed directly by Northern blot analysis with RNA from the RNase P TS mutants. Numerous potential substrates were identified, of which we characterized the box C/D intron-encoded small nucleolar RNAs (snoRNAs), because these both copurify with RNase P and accumulate larger forms in the RNase P temperature-sensitive mutants. It was previously known that two pathways existed for excising these snoRNAs, one using the pre-mRNA splicing path and the other that was independent of splicing. RNase P appears to participate in the splicing-independent path for the box C/D intron-encoded snoRNAs.
机译：核糖核酸酶P（RNase P）是必需的核酸内切酶，负责前体tRNA的5'端成熟。细菌RNase P还处理前体4.5S RNA，tmRNA，30S核糖体前RNA和一些报道的蛋白质编码RNA。真核核糖核酸酶P比细菌形式的复杂得多，除催化RNA亚基外还使用多个必需蛋白质亚基。 RNomic研究表明，除了tRNA以外，RNase P还与其他RNA结合，但以前尚未鉴定出非tRNA底物。通过在发芽的酵母酿酒酵母中使用多管齐下的方法鉴定了其他底物。首先，通过使用在两个必不可少的RNase P亚基Pop1p和Rpr1r中包含温度敏感（TS）突变的菌株，在全基因组微阵列上检查了RNase P依赖性的RNA丰度变化。其次，RNA酶P被快速亲和纯化，并通过使用全基因组微阵列鉴定出纯化的RNA。第三，为了鉴定当RNase P耗尽时不会改变丰度而是积累为较大前体的RNA，可通过Northern印迹分析，用来自RNase P TS突变体的RNA直接探测> 80个潜在的小RNA底物。确定了许多潜在的底物，我们对它们进行了盒C / D内含子编码小核仁RNA（snoRNA）的表征，因为它们都与RNase P共纯化并且在RNase P温度敏感突变体中积累较大形式。先前已知存在两种切除这些snoRNA的途径，一种途径使用pre-mRNA剪接路径，另一种途径与剪接无关。 RNase P似乎参与了盒C / D内含子编码snoRNA的非剪接路径。

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