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RNA解旋酶样蛋白PRP22从剪接体释放信使核糖核酸的需求。

Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes.

作者信息

Company M, Arenas J, Abelson J

机构信息

Division of Biology, California Institute of Technology, Pasadena 91125.

出版信息

Nature. 1991 Feb 7;349(6309):487-93. doi: 10.1038/349487a0.

Abstract

The product of the yeast PRP22 gene acts late in the splicing of yeast pre-messenger RNA, mediating the release of the spliced mRNA from the spliceosome. The predicted PRP22 protein sequence shares extensive homology with that of PRP2 and PRP16 proteins, which are also involved in nuclear pre-mRNA splicing. The homologous region contains sequence elements characteristic of several demonstrated or putative ATP-dependent RNA helicases. A putative RNA-binding motif originally identified in bacterial ribosomal protein S1 and Escherichia coli polynucleotide phosphorylase has also been found in PRP22.

摘要

酵母PRP22基因的产物在酵母前体信使RNA的剪接后期发挥作用,介导剪接后的mRNA从剪接体中释放出来。预测的PRP22蛋白序列与PRP2和PRP16蛋白的序列具有广泛的同源性,PRP2和PRP16蛋白也参与核前体mRNA的剪接。同源区域包含几种已证实的或推测的ATP依赖性RNA解旋酶的特征性序列元件。最初在细菌核糖体蛋白S1和大肠杆菌多核苷酸磷酸化酶中鉴定出的一个推测的RNA结合基序,也在PRP22中被发现。

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