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真核生物硒代半胱氨酸插入tRNA种类支持大肠杆菌中的硒蛋白合成。

Eukaryotic selenocysteine inserting tRNA species support selenoprotein synthesis in Escherichia coli.

作者信息

Baron C, Sturchler C, Wu X Q, Gross H J, Krol A, Böck A

机构信息

Lehrstuhl für Mikrobiologie, Universität München, Germany.

出版信息

Nucleic Acids Res. 1994 Jun 25;22(12):2228-33. doi: 10.1093/nar/22.12.2228.

DOI:10.1093/nar/22.12.2228
PMID:8036149
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC523678/
Abstract

Although the tRNA species directing selenocysteine insertion in prokaryotes differ greatly in their primary structure from that of their eukaryotic homologues they share very similar three-dimensional structures. To analyse whether this conservation of the overall shape of the molecules reflects a conservation of their functional interactions it was tested whether the selenocysteine inserting tRNA species from Homo sapiens supports selenoprotein synthesis in E. coli. It was found that the expression of the human tRNA(Sec) gene in E.coli can complement a lesion in the tRNA(Sec) gene of this organism. Transcripts of the Homo sapiens and Xenopus laevis tRNA(Sec) genes synthesised in vitro were amino-acylated by the E.coli seryl-tRNA ligase although at a very low rate and the resulting seryl-tRNA(Sec) was bound to and converted into selenocysteyl-tRNA(Sec) by the selenocysteine synthase of this organism. Selenocysteyl-tRNA(Sec) from both eukaryotes was able to form a complex with translation factor SELB from E.coli. Although the mechanism of selenocysteine incorporation into seleno-proteins appears to be rather different in E.coli and in vertebrates, we observe here a surprising conservation of functions over an enormous evolutionary distance.

摘要

尽管在原核生物中指导硒代半胱氨酸插入的tRNA种类在一级结构上与真核生物的同源物有很大差异,但它们具有非常相似的三维结构。为了分析分子整体形状的这种保守性是否反映了其功能相互作用的保守性,研究人员测试了来自智人的硒代半胱氨酸插入tRNA种类是否支持大肠杆菌中的硒蛋白合成。结果发现,人tRNA(Sec)基因在大肠杆菌中的表达可以弥补该生物体tRNA(Sec)基因的缺陷。在体外合成的智人和非洲爪蟾tRNA(Sec)基因的转录本被大肠杆菌丝氨酰-tRNA连接酶氨酰化,尽管速率非常低,并且产生的丝氨酰-tRNA(Sec)被该生物体的硒代半胱氨酸合酶结合并转化为硒代半胱氨酰-tRNA(Sec)。来自两种真核生物的硒代半胱氨酰-tRNA(Sec)都能够与大肠杆菌的翻译因子SELB形成复合物。尽管在大肠杆菌和脊椎动物中,硒代半胱氨酸掺入硒蛋白的机制似乎有很大不同,但我们在此观察到,在巨大的进化距离上,功能存在惊人的保守性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fefb/523678/8a28539c8084/nar00036-0058-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fefb/523678/29f1a1595323/nar00036-0057-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fefb/523678/8a28539c8084/nar00036-0058-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fefb/523678/29f1a1595323/nar00036-0057-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fefb/523678/8a28539c8084/nar00036-0058-a.jpg

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本文引用的文献

1
Solution structure of selenocysteine-inserting tRNA(Sec) from Escherichia coli. Comparison with canonical tRNA(Ser).来自大肠杆菌的插入硒代半胱氨酸的tRNA(Sec)的溶液结构。与典型tRNA(Ser)的比较。
J Mol Biol. 1993 May 20;231(2):274-92. doi: 10.1006/jmbi.1993.1282.
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Interaction of translation factor SELB with the formate dehydrogenase H selenopolypeptide mRNA.翻译因子SELB与甲酸脱氢酶H硒代多肽mRNA的相互作用。
Proc Natl Acad Sci U S A. 1993 May 1;90(9):4181-5. doi: 10.1073/pnas.90.9.4181.
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Unique secondary and tertiary structural features of the eucaryotic selenocysteine tRNA(Sec).
Acta Biochim Biophys Sin (Shanghai). 2008 Jul;40(7):539-53. doi: 10.1111/j.1745-7270.2008.00435.x.
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From one amino acid to another: tRNA-dependent amino acid biosynthesis.从一种氨基酸到另一种氨基酸:依赖于转运RNA的氨基酸生物合成
Nucleic Acids Res. 2008 Apr;36(6):1813-25. doi: 10.1093/nar/gkn015. Epub 2008 Feb 5.
5
Selenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factors.硒代半胱氨酸tRNA特异性延伸因子SelB是延伸因子和起始因子的结构嵌合体。
EMBO J. 2005 Jan 12;24(1):11-22. doi: 10.1038/sj.emboj.7600505. Epub 2004 Dec 23.
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Barriers to heterologous expression of a selenoprotein gene in bacteria.细菌中硒蛋白基因异源表达的障碍。
J Bacteriol. 1997 Feb;179(3):576-82. doi: 10.1128/jb.179.3.576-582.1997.
真核生物硒代半胱氨酸转运RNA(Sec)独特的二级和三级结构特征。
Nucleic Acids Res. 1993 Mar 11;21(5):1073-9. doi: 10.1093/nar/21.5.1073.
4
Conserved nucleotide sequences in the open reading frame and 3' untranslated region of selenoprotein P mRNA.硒蛋白P信使核糖核酸开放阅读框和3'非翻译区中的保守核苷酸序列。
Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):537-41. doi: 10.1073/pnas.90.2.537.
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EMBO J. 1993 Aug;12(8):3333-8. doi: 10.1002/j.1460-2075.1993.tb06003.x.
6
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EMBO J. 1993 Aug;12(8):3315-22. doi: 10.1002/j.1460-2075.1993.tb06001.x.
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8
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EMBO J. 1994 Jan 1;13(1):241-8. doi: 10.1002/j.1460-2075.1994.tb06254.x.
9
The long extra arms of human tRNA((Ser)Sec) and tRNA(Ser) function as major identify elements for serylation in an orientation-dependent, but not sequence-specific manner.人tRNA((Ser)Sec)和tRNA(Ser)的长额外臂作为丝氨酰化的主要识别元件,以方向依赖但非序列特异性的方式起作用。
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10
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J Biol Chem. 1993 Nov 5;268(31):23128-31.