Structural and functional analysis of Utp24, an endonuclease for processing 18S ribosomal RNA.

Structural and functional analysis of Utp24, an endonuclease for processing 18S ribosomal RNA.
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Utp24(一种用于处理 18S 核糖体 RNA 的核酸内切酶)的结构和功能分析。

DOI:
10.1371/journal.pone.0195723
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发表时间:
2018
期刊:
影响因子:
3.7
通讯作者:
Ye K
Ye K
中科院分区:
综合性期刊3区
文献类型:
--
作者:
An W;Du Y;Ye K

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前体核糖体RNA通过多个步骤的溶核切割加工以产生成熟的rRNA。Utp 24是核糖体小亚基前体90 S早期的PIN结构域内切酶,被认为在前体rRNA的A1和A2位点切割。在这里,我们确定的Utp 24的晶体结构裂殖酵母粟酒裂殖酵母在2.1埃分辨率。Utp 24在结构上类似于核糖体组装因子Utp 23,并且都含有锌指基序。在酿酒酵母中的功能分析表明,Utp 24的耗尽扰乱了90 S的组装,并取消了在A0,A1和A2位点的切割。与失活的Utp 24组装的90 S在A0-切割后状态下停滞,并含有富集的核外泌体用于降解5' ETS。尽管Utp 24具有很高的序列保守性,但其他生物的Utp 24在S.这表明Utp 24需要精确定位在90 S。我们的研究为Utp 24在90 S组装和活性中的作用提供了生化和结构方面的见解。
The precursor ribosomal RNA is processed by multiple steps of nucleolytic cleavage to generate mature rRNAs. Utp24 is a PIN domain endonuclease in the early 90S precursor of small ribosomal subunit and is proposed to cleave at sites A1 and A2 of pre-rRNA. Here we determine the crystal structure of Utp24 from Schizosaccharomyces pombe at 2.1 angstrom resolution. Utp24 structurally resembles the ribosome assembly factor Utp23 and both contain a Zn-finger motif. Functional analysis in Saccharomyces cerevisiae shows that depletion of Utp24 disturbs the assembly of 90S and abolishes cleavage at sites A0, A1 and A2. The 90S assembled with inactivated Utp24 is arrested at a post-A0-cleavage state and contains enriched nuclear exosome for degradation of 5' ETS. Despite of high sequence conservation, Utp24 from other organisms is unable to form an active 90S in S. cerevisiae, suggesting that Utp24 needs to be precisely positioned in 90S. Our study provides biochemical and structural insight into the role of Utp24 in 90S assembly and activity.
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