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谷氨酰-脯氨酰-tRNA合成酶(EPRS)结构与功能的新认识 被引量:2

New insights on the structure and function of glutamyl-prolyl-tRNA synthetase
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摘要 氨基酰-tRNA合成酶(ARS)催化特异的氨基酸结合到对应tRNA上,确保mRNA高精度地翻译为蛋白质。最近陆续报道ARS同时也在细胞基本生命活动如RNA运输、转录、翻译、免疫反应以及血管生成中充当重要的调节分子和活性成分。目前报道谷氨酰-脯氨酰-tRNA合成酶(EPRS)在具有催化谷氨酸和脯氨酸分别结合到不同tRNA上的功能之外,还可通过基因选择性沉默机制阻遏血浆铜蓝蛋白的表达,从而终止炎症反应等。本文就该酶结构与功能的研究新进展进行综述,并对其进行分子进化分析。 Aminoacyl-tRNA synthetases catalyze the attachment of specific amino acids to cognate transfer RNAs, which ensure the high fidelity of transferring genetic information from DNA into protein. Recent studies show that aminoacyl-tRNA synthetases play important roles in cell life, such as taking part in intracellular RNA degrading, mRNA splicing, gene transcription regulation, immune response and angiogenesis. In addition to be a bifunctinal aminoacyl-tRNA synthetase to catalyze the attachment of glutamic acid and proline to cognate tRNA respectively, glutamyl-prolyl-tRNA synthetase (EPRS) was recently reported to regulate the expression of ceruloplasmin by selective silence mechanism, and to block the injury caused by inflammation response. The structure and novel functions of EPRS are summarized.
出处 《军事医学科学院院刊》 CSCD 北大核心 2006年第2期166-168,200,共4页 Bulletin of the Academy of Military Medical Sciences
基金 国家自然科学基金重大研究计划项目(90208017) 国家自然科学基金面上项目(30400465 30300358) 军事医学科学院科技创新启动基金(0402013)资助
关键词 氨基酰-TRNA合成酶 双功能氨基酰-tRNA合成酶 谷氨酰-脯氨酰-tRNA合成酶 aminoacyl-tRNA synthetase bifunctinal aminoacyl-tRNA synthetase glutamyl-prolyl-tRNA synthetase
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  • 1Szymanski M,Deniziak M,Barciszewski J.The new aspects of aminoacyl-tRNA synthetases[J].Acta Biochim Pol,2000,47(3):821-834.
  • 2Rho SB,Kim MJ,Lee JS,et al.Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex[J].Proc Natl Acad Sci USA,1999,96(8):4488-4493.
  • 3Lee SW,Cho BH,Park SG,et al.Aminoacyl-tRNA synthetase complexes:beyond translation[J].J Cell Sci,2004,117(17):3725-3734.
  • 4Cerni C,Kerjan P,Astier M,et al.A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase[J].EMBO J,1991,10(13):4267-4277.
  • 5Berthonneau E,Mirande M.A gene fusion event in the evolution of aminoacyl-tRNA synthetases[J].FEBS Lett,2000,470(3):300-304.
  • 6Jeong EJ,Hwang GS,Kim KH,et al.Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase:identification of RNA-binding residues and functional implications for tandem repeats[J].Biochemistry,2000,39(51):15775-15782.
  • 7Quevillon S,Robinson JC,Berthonneau E,et al.Macromolecular assemblage of aminoacyl-tRNA synthetases:identification of protein-protein interactions and characterization of a core protein[J].J Mol Biol,1999,285(1):183-195.
  • 8Cahuzac B,Berthonneau E,Birlirakis N,et al.A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases[J].EMBO J,2000,19(3):445-452.
  • 9Stehlin C,Burke B,Yang F,et al.Species-specific differences in the operational RNA code for aminoacylation of tRNAPro[J].Biochemistry,1998,37(23):8605-8613.
  • 10Martinis SA,Plateau P,Cavarelli J,et al.Aminoacyl-tRNA synthetases:a family of expanding functions[J].EMBO J,1999,18(17):4591-4596.

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