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2
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Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis.聚腺苷酸聚合酶的作用机制:酶-MgATP-RNA三元复合物的结构及动力学分析
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本文引用的文献

1
A history of poly A sequences: from formation to factors to function.多聚腺苷酸序列的历史:从形成到相关因子再到功能
Prog Nucleic Acid Res Mol Biol. 2002;71:285-389. doi: 10.1016/s0079-6603(02)71046-5.
2
Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase.一种不依赖模板的DNA聚合酶——小鼠末端脱氧核苷酸转移酶的晶体结构
EMBO J. 2002 Feb 1;21(3):427-39. doi: 10.1093/emboj/21.3.427.
3
Fip1 regulates the activity of Poly(A) polymerase through multiple interactions.Fip1通过多种相互作用调节聚腺苷酸聚合酶的活性。
Mol Cell Biol. 2001 Mar;21(6):2026-37. doi: 10.1128/MCB.21.6.2026-2037.2001.
4
Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP.单独的酵母聚腺苷酸聚合酶及其与3'-dATP复合物的结构。
Science. 2000 Aug 25;289(5483):1346-9. doi: 10.1126/science.289.5483.1346.
5
Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP.与ATP类似物结合的哺乳动物聚腺苷酸聚合酶的晶体结构。
EMBO J. 2000 Aug 15;19(16):4193-203. doi: 10.1093/emboj/19.16.4193.
6
Mapping of ATP binding regions in poly(A) polymerases by photoaffinity labeling and by mutational analysis identifies a domain conserved in many nucleotidyltransferases.通过光亲和标记和突变分析对聚腺苷酸聚合酶中ATP结合区域进行定位,确定了在许多核苷酸转移酶中保守的一个结构域。
Protein Sci. 1999 Nov;8(11):2380-91. doi: 10.1110/ps.8.11.2380.
7
An open and closed case for all polymerases.关于所有聚合酶的一个公开与已了结的案例。
Structure. 1999 Feb 15;7(2):R31-5. doi: 10.1016/S0969-2126(99)80017-3.
8
Formation of mRNA 3' ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis.真核生物中mRNA 3'末端的形成:机制、调控及其与mRNA合成其他步骤的相互关系
Microbiol Mol Biol Rev. 1999 Jun;63(2):405-45. doi: 10.1128/MMBR.63.2.405-445.1999.
9
Processivity of the Saccharomyces cerevisiae poly(A) polymerase requires interactions at the carboxyl-terminal RNA binding domain.酿酒酵母多聚腺苷酸聚合酶的持续合成能力需要在羧基末端RNA结合结构域进行相互作用。
Mol Cell Biol. 1998 Oct;18(10):5942-51. doi: 10.1128/MCB.18.10.5942.
10
CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: characterization of the CCA-adding enzyme from the archaeal hyperthermophile Sulfolobus shibatae.添加CCA的酶和聚腺苷酸聚合酶都是同一核苷酸转移酶超家族的成员:来自嗜热古菌柴田硫化叶菌的添加CCA的酶的特性
RNA. 1996 Sep;2(9):895-908.

酵母聚腺苷酸聚合酶中间结构域的突变会影响其与RNA的相互作用,但不影响与ATP的相互作用。

Mutations in the middle domain of yeast poly(A) polymerase affect interactions with RNA but not ATP.

作者信息

Zhelkovsky Alexander, Helmling Steffen, Bohm Andrew, Moore Claire

机构信息

Tufts University School of Medicine and Sackler School of Graduate Biomedical Sciences, Boston, Massachusetts 02111, USA.

出版信息

RNA. 2004 Apr;10(4):558-64. doi: 10.1261/rna.5238704.

DOI:10.1261/rna.5238704
PMID:15037764
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1370545/
Abstract

The eukaryotic poly(A) polymerase (PAP) is responsible for the posttranscriptional extension of mRNA 3' ends by the addition of a poly(A) tract. The recently published three-dimensional structures of yeast and bovine PAPs have made a more directed biochemical analysis of this enzyme possible. Based on these structures, the middle domain of PAP was predicted to interact with ATP. However, in this study, we show that mutations of conserved residues in this domain of yeast PAP, Pap1, do not affect interaction with ATP, but instead disrupt the interaction with RNA and affect the enzyme's ability to process substrate lacking 2' hydroxyls at the 3' end. These results are most consistent with a model in which the middle domain of PAP interacts directly with the recently extended RNA and pyrophosphate byproduct.

摘要

真核生物多聚腺苷酸聚合酶(PAP)负责通过添加多聚腺苷酸尾在转录后延伸mRNA的3'末端。最近发表的酵母和牛PAP的三维结构使得对该酶进行更有针对性的生化分析成为可能。基于这些结构,预测PAP的中间结构域与ATP相互作用。然而,在本研究中,我们表明酵母PAP(Pap1)该结构域中保守残基的突变并不影响与ATP的相互作用,而是破坏与RNA的相互作用,并影响该酶处理3'末端缺乏2'羟基底物的能力。这些结果与一个模型最为一致,在该模型中,PAP的中间结构域直接与最近延伸的RNA和焦磷酸副产物相互作用。