Structural insight into precursor ribosomal RNA processing by ribonuclease MRP

doi:10.1126/science.abc0149

GSTDTAP > 气候变化

DOI	10.1126/science.abc0149
	Structural insight into precursor ribosomal RNA processing by ribonuclease MRP
	Pengfei Lan; Bin Zhou; Ming Tan; Shaobai Li; Mi Cao; Jian Wu; Ming Lei
	2020-08-07
发表期刊	Science
出版年	2020
英文摘要	RNA-based catalysts perform fundamental tasks in cellular RNA metabolism, especially in eukaryotes, where RNAs are cut by specialized ribonucleoproteins (RNPs) as part of ribosome assembly or messenger RNA regulation or splicing. Both RNA and protein components play a role in shaping how these large catalytic complexes interact with their RNA substrates. Lan et al. determined the cryo–electron microscopy structures of a yeast RNP called ribonuclease MRP both alone and bound to a small RNA substrate. Comparison with the related ribonuclease P revealed differences in both protein and RNA components that enable ribonuclease MRP to recognize substrates with a specific sequence motif, rather than purely recognizing RNA structure as ribonuclease P does. These structures aid in considering how RNPs evolved and why they remain central to eukaryotic RNA processing. Science , this issue p. [656][1] Ribonuclease (RNase) MRP is a conserved eukaryotic ribonucleoprotein complex that plays essential roles in precursor ribosomal RNA (pre-rRNA) processing and cell cycle regulation. In contrast to RNase P, which selectively cleaves transfer RNA–like substrates, it has remained a mystery how RNase MRP recognizes its diverse substrates. To address this question, we determined cryo–electron microscopy structures of Saccharomyces cerevisiae RNase MRP alone and in complex with a fragment of pre-rRNA. These structures and the results of biochemical studies reveal that coevolution of both protein and RNA subunits has transformed RNase MRP into a distinct ribonuclease that processes single-stranded RNAs by recognizing a short, loosely defined consensus sequence. This broad substrate specificity suggests that RNase MRP may have myriad yet unrecognized substrates that could play important roles in various cellular contexts. [1]: /lookup/doi/10.1126/science.abc0149
领域	气候变化 ; 资源环境
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文献类型	期刊论文
条目标识符	http://119.78.100.173/C666/handle/2XK7JSWQ/288002
专题	气候变化资源环境科学
推荐引用方式 GB/T 7714	Pengfei Lan,Bin Zhou,Ming Tan,et al. Structural insight into precursor ribosomal RNA processing by ribonuclease MRP[J]. Science,2020.
APA	Pengfei Lan.,Bin Zhou.,Ming Tan.,Shaobai Li.,Mi Cao.,...&Ming Lei.(2020).Structural insight into precursor ribosomal RNA processing by ribonuclease MRP.Science.
MLA	Pengfei Lan,et al."Structural insight into precursor ribosomal RNA processing by ribonuclease MRP".Science (2020).