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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >An intrinsically disordered C terminus allows the La protein to assist the biogenesis of diverse noncoding RNA precursors
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An intrinsically disordered C terminus allows the La protein to assist the biogenesis of diverse noncoding RNA precursors

机译：本质上无序的C末端允许La蛋白协助多种非编码RNA前体的生物发生

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摘要

The La protein binds the 3' ends of many newly synthesized non-coding RNAs, protecting these RNAs from nucleases and influencing folding, maturation, and ribonucleoprotein assembly. Although 3' end binding by La involves the N-terminal La domain and adjacent RNA recognition motif (RRM), the mechanisms by which La stabilizes diverse RNAs from nucleases and assists subsequent events in their biogenesis are unknown. Here we report that a conserved feature of La proteins, an intrinsically disordered C terminus, is required for the accumulation of certain noncoding RNA precursors and for the role of the Saccharomyces cerevisiae La protein Lhp1p in assisting formation of correctly folded pre-tRNA anticodon stems in vivo. Footprinting experiments using purified Lhpip reveal that the C terminus is required to protect a pre-tRNA anticodon stem from chemical modification. Although the C terminus of Lhpip is hypersensitive to proteases in vitro, it becomes protease-resistant upon binding pre-tRNAs, U6 RNA, or pre-5S rRNA. Thus, while high affinity binding to 3' ends requires the La domain and RRM, a con-formationally flexible C terminus allows La to interact productively with a diversity of noncoding RNA precursors. We propose that intrinsically disordered domains adjacent to well characterized RNA-binding motifs in other promiscuous RNA-binding proteins may similarly contribute to the ability of these proteins to influence the cellular fates of multiple distinct RNA targets.
机译：La蛋白与许多新合成的非编码RNA的3'末端结合，保护这些RNA不受核酸酶的影响，并影响折叠，成熟和核糖核蛋白的组装。尽管La与3'端结合涉及N端La结构域和相邻的RNA识别基序（RRM），但La稳定核酸酶中各种RNA并协助其生物发生的后续事件的机制尚不清楚。在这里我们报告一个固有的无序C端La蛋白的保守特征是某些非编码RNA前体的积累和酿酒酵母La蛋白Lhp1p在协助正确折叠前tRNA反密码子茎形成中的作用所必需的体内。使用纯化的Lhpip进行的足迹实验表明，需要C末端来保护pre-tRNA反密码子茎免受化学修饰。尽管Lhpip的C末端在体外对蛋白酶过敏，但在结合pre-tRNA，U6 RNA或pre-5S rRNA时，它对蛋白酶具有抗性。因此，虽然与3'端的高亲和力结合需要La结构域和RRM，但构型灵活的C末端允许La与多种非编码RNA前体有效地相互作用。我们提出与其他混杂RNA结合蛋白中特征明确的RNA结合基序相邻的内在无序域可能会类似地有助于这些蛋白影响多个不同RNA靶标的细胞命运的能力。

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