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一种来自酿酒酵母的与tRNA剪接有关的高度特异性磷酸酶。

A highly specific phosphatase from Saccharomyces cerevisiae implicated in tRNA splicing.

作者信息

McCraith S M, Phizicky E M

机构信息

Department of Biochemistry, University of Rochester School of Medicine and Dentistry, New York 14642.

出版信息

Mol Cell Biol. 1990 Mar;10(3):1049-55. doi: 10.1128/mcb.10.3.1049-1055.1990.

DOI:10.1128/mcb.10.3.1049-1055.1990
PMID:2154680
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC360964/
Abstract

We identified and partially purified a phosphatase from crude extracts of Saccharomyces cerevisiae cells that can catalyze the last step of tRNA splicing in vitro. This phosphatase can remove the 2'-phosphate left over at the splice junction after endonuclease has removed the intron and ligase has joined together the two half-molecules. We suggest that this phosphatase is responsible for the completion of tRNA splicing in vivo, based primarily on its specificity for the 2'-phosphate of spliced tRNA and on the resistance of the splice junction 2'-phosphate to a nonspecific phosphatase. Removal of the splice junction 2'-phosphate from the residue adjacent to the anticodon is likely necessary for efficient expression of spliced tRNA. The phosphatase appears to be composed of at least two components which, together with endonuclease and ligase, can be used to reconstitute the entire tRNA-splicing reaction.

摘要

我们从酿酒酵母细胞的粗提物中鉴定并部分纯化了一种磷酸酶，该磷酸酶能够在体外催化tRNA剪接的最后一步。这种磷酸酶可以去除核酸内切酶切除内含子且连接酶将两个半分子连接在一起后，在剪接位点留下的2'-磷酸基团。我们认为，这种磷酸酶负责体内tRNA剪接的完成，这主要基于其对剪接后tRNA的2'-磷酸基团的特异性，以及剪接位点2'-磷酸基团对非特异性磷酸酶的抗性。从反密码子相邻的残基上去除剪接位点2'-磷酸基团，对于剪接后tRNA的有效表达可能是必要的。该磷酸酶似乎至少由两个组分组成，它们与核酸内切酶和连接酶一起，可用于重构整个tRNA剪接反应。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2da6/360964/ceb9538d1275/molcellb00039-0202-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2da6/360964/4c2ab005348e/molcellb00039-0199-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2da6/360964/d0a4b72ddc0f/molcellb00039-0200-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2da6/360964/2c3d062d85c3/molcellb00039-0201-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2da6/360964/ceb9538d1275/molcellb00039-0202-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2da6/360964/4c2ab005348e/molcellb00039-0199-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2da6/360964/d0a4b72ddc0f/molcellb00039-0200-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2da6/360964/2c3d062d85c3/molcellb00039-0201-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2da6/360964/ceb9538d1275/molcellb00039-0202-a.jpg

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Formation of a 2'-phosphomonoester, 3',5'-phosphodiester linkage by a novel RNA ligase in wheat germ.小麦胚芽中一种新型RNA连接酶形成2'-磷酸单酯、3',5'-磷酸二酯键。
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Enzymatic mechanism of an RNA ligase from wheat germ.
真菌 tRNA 连接酶对 2'-磷酸末端需求的动力学和结构见解。
RNA. 2024 Sep 16;30(10):1306-1314. doi: 10.1261/rna.080120.124.
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Characterization of tRNA splicing enzymes RNA ligase and tRNA 2'-phosphotransferase from the pathogenic fungi Mucorales.从致病真菌毛霉目中鉴定 tRNA 剪接酶 RNA 连接酶和 tRNA 2′-磷酸转移酶。
RNA. 2024 Mar 18;30(4):367-380. doi: 10.1261/rna.079911.123.
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Structural basis for Tpt1-catalyzed 2'-PO transfer from RNA and NADP(H) to NAD.Tpt1 催化 RNA 和 NADP(H)向 NAD 的 2'-PO 转移的结构基础。
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