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1
The ribosomal binding and peptidyl-tRNA hydrolysis functions of Escherichia coli release factor 2 are linked through residue 246.大肠杆菌释放因子2的核糖体结合功能和肽基-tRNA水解功能通过246位残基相联系。
RNA. 2000 Dec;6(12):1704-13. doi: 10.1017/s135583820000131x.
2
The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis.人类真核释放因子eRF1的晶体结构——终止密码子识别及肽基-tRNA水解机制
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3
A single proteolytic cleavage in release factor 2 stabilizes ribosome binding and abolishes peptidyl-tRNA hydrolysis activity.释放因子2中的单次蛋白水解切割可稳定核糖体结合并消除肽基-tRNA水解活性。
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4
A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis.核糖体释放因子在蛋白质合成终止过程中诱导肽基 - tRNA 裂解的机制模型。
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6
Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis.1类多肽释放因子高度保守的GGQ基序中的突变消除了人eRF1触发肽基-tRNA水解的能力。
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Functional specificity of amino acid at position 246 in the tRNA mimicry domain of bacterial release factor 2.细菌释放因子2的tRNA模拟结构域中第246位氨基酸的功能特异性
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8
Stop codon recognition and interactions with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from Escherichia coli.来自大肠杆菌的截短型和嵌合型RF1及RF2的终止密码子识别以及与肽释放因子RF3的相互作用。
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Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition.1类翻译终止因子:不变的GGQ小结构域对释放活性和核糖体结合至关重要,但对终止密码子识别并非如此。
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Codon reassignment to facilitate genetic engineering and biocontainment in the chloroplast of Chlamydomonas reinhardtii.密码子重新分配以促进莱茵衣藻叶绿体中的基因工程和生物防护。
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8
Common and specific amino acid residues in the prokaryotic polypeptide release factors RF1 and RF2: possible functional implications.原核生物多肽释放因子RF1和RF2中的常见和特定氨基酸残基:可能的功能意义。
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9
HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination.HemK是一类与DNA甲基转移酶相似的蛋白质甲基转移酶,它能使多肽链释放因子发生甲基化,并且HemK基因敲除会导致翻译终止缺陷。
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10
A dynamic competition between release factor 2 and the tRNA(Sec) decoding UGA at the recoding site of Escherichia coli formate dehydrogenase H.在大肠杆菌甲酸脱氢酶H的重编码位点,释放因子2与解码UGA的tRNA(Sec)之间的动态竞争。
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本文引用的文献

1
A tripeptide 'anticodon' deciphers stop codons in messenger RNA.一种三肽“反密码子”可解读信使核糖核酸中的终止密码子。
Nature. 2000 Feb 10;403(6770):680-4. doi: 10.1038/35001115.
2
The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis.人类真核释放因子eRF1的晶体结构——终止密码子识别及肽基-tRNA水解机制
Cell. 2000 Feb 4;100(3):311-21. doi: 10.1016/s0092-8674(00)80667-4.
3
Macromolecular mimicry.大分子模拟
EMBO J. 2000 Feb 15;19(4):489-95. doi: 10.1093/emboj/19.4.489.
4
Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis.1类多肽释放因子高度保守的GGQ基序中的突变消除了人eRF1触发肽基-tRNA水解的能力。
RNA. 1999 Aug;5(8):1014-20. doi: 10.1017/s135583829999043x.
5
Indirect regulation of translational termination efficiency at highly expressed genes and recoding sites by the factor recycling function of Escherichia coli release factor RF3.通过大肠杆菌释放因子RF3的因子循环功能对高表达基因和重编码位点的翻译终止效率进行间接调控。
EMBO J. 1999 Feb 1;18(3):727-32. doi: 10.1093/emboj/18.3.727.
6
A direct estimation of the context effect on the efficiency of termination.对终止效率的背景效应的直接估计。
J Mol Biol. 1998 Dec 4;284(3):579-90. doi: 10.1006/jmbi.1998.2220.
7
Initiation factors of protein biosynthesis in bacteria and their structural relationship to elongation and termination factors.细菌中蛋白质生物合成的起始因子及其与延伸和终止因子的结构关系。
Mol Microbiol. 1998 Jul;29(2):409-17. doi: 10.1046/j.1365-2958.1998.00893.x.
8
Efficient in vitro translational termination in Escherichia coli is constrained by the orientations of the release factor, stop signal and peptidyl-tRNA within the termination complex.大肠杆菌中高效的体外翻译终止受到终止复合物中释放因子、终止信号和肽基-tRNA方向的限制。
Biol Chem. 1998 Jul;379(7):857-66. doi: 10.1515/bchm.1998.379.7.857.
9
How protein reads the stop codon and terminates translation.蛋白质如何识别终止密码子并终止翻译。
Genes Cells. 1998 May;3(5):265-78. doi: 10.1046/j.1365-2443.1998.00191.x.
10
Mutations in RNAs of both ribosomal subunits cause defects in translation termination.两个核糖体亚基的RNA发生突变会导致翻译终止缺陷。
EMBO J. 1998 Mar 2;17(5):1507-14. doi: 10.1093/emboj/17.5.1507.

大肠杆菌释放因子2的核糖体结合功能和肽基-tRNA水解功能通过246位残基相联系。

The ribosomal binding and peptidyl-tRNA hydrolysis functions of Escherichia coli release factor 2 are linked through residue 246.

作者信息

Wilson D N, Guévremont D, Tate W P

机构信息

Department of Biochemistry and Centre for Gene Research, University of Otago, Dunedin, New Zealand.

出版信息

RNA. 2000 Dec;6(12):1704-13. doi: 10.1017/s135583820000131x.

DOI:10.1017/s135583820000131x
PMID:11142371
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1370041/
Abstract

Replacing a cassette of 31 residues from Escherichia coli release factor 1 with the equivalent residues in release factor 2 gave a protein active in codon-specific binding to the ribosome but inactive in peptidyl-tRNA hydrolysis. Such a phenotype is also found unexpectedly with release factor 2 when expressed at high concentration in bacteria. Substituting threonine with the release factor 1 equivalent serine at position 246 within the cassette restored the impaired activity of the chimeric protein, and also that of inactive recombinant release factor 2, both in vitro and in vivo. The differences in activity are not due to posttranslational modifications or a lack of it at this residue. Random mutagenesis of codon 246 suggests that this position is pivotal for the function of the release factor, being able to affect differentially both its binding to the ribosome and its peptide release activities. We propose that amino acid 246 is close to a sharp turn (GGQ motif at position 250), and is essential for transmitting the signal from cognate codon recognition by correctly positioning the peptidyl-tRNA hydrolysis domain of the release factor into the peptidyltransferase center.

摘要

将大肠杆菌释放因子1的一段31个残基的片段替换为释放因子2中的等效残基,得到了一种在密码子特异性结合核糖体方面具有活性,但在肽基-tRNA水解方面无活性的蛋白质。当在细菌中高浓度表达时,释放因子2也意外地出现了这种表型。在该片段内的第246位将苏氨酸替换为释放因子1中的等效丝氨酸——丝氨酸,恢复了嵌合蛋白受损的活性,以及无活性的重组释放因子2在体外和体内的活性。活性差异并非由于该残基的翻译后修饰或缺乏翻译后修饰。对密码子246进行随机诱变表明,该位置对于释放因子的功能至关重要,能够分别影响其与核糖体的结合及其肽释放活性。我们提出,氨基酸246靠近一个急转弯(第250位的GGQ基序),并且对于通过将释放因子的肽基-tRNA水解结构域正确定位到肽基转移酶中心来传递来自同源密码子识别的信号至关重要。