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Crystal structure of a reverse polymerase

机译:反向聚合酶的晶体结构

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摘要

The primary transcripts of transfer RNA (tRNA) molecules undergo extensive processing and chemical modification to become functional components of the protein synthesis apparatus. Some of these reactions are common to all tRNAs in a particular cell, whereas others are specific to a subset of the species or even to just a single amino-acid-accepting class (1). In some organisms the maturation of histi-dine-specific tRNAs (tRNAHis) includes the unique addition of guanosine (G-1) to the 5' terminus of tRNA (2). This G-1 addition step is a phosphodiester bond formation reaction that operates in a unique 3'-5' direction, opposite to all conventional DNA and RNA polymerases. In PNAS, Hyde et al. (3) unveil crystal structures of a Thg1 enzyme that catalyzes G-1 addition. The structures show that the catalytic domain of Thgl shares both a common architecture and a two-metal ion-dependent mechanism with canonical 5'-3' DNA polymerases. These remarkable findings open new vistas in tRNA enzy-mology and the evolution of nucleic acid polymerases.
机译:转移RNA(tRNA)分子的主要转录本经过大量加工和化学修饰,成为蛋白质合成装置的功能组件。这些反应中的某些反应是特定细胞中所有tRNA的共同反应,而其他反应则是特定于该物种的一个子集,甚至仅是单个接受氨基酸的类别(1)。在某些生物中,组氨酸特异性tRNA(tRNAHis)的成熟包括将鸟苷(G-1)独特地添加到tRNA的5'末端(2)。该G-1加成步骤是磷酸二酯键形成反应,其以独特的3'-5'方向进行,与所有常规DNA和RNA聚合酶相反。在PNAS中,Hyde等人。 (3)揭示了催化G-1加成的Thg1酶的晶体结构。该结构表明,Thgl的催化结构域与5'-3'DNA规范化酶具有共同的结构和双金属离子依赖性机制。这些非凡的发现为tRNA酶学和核酸聚合酶的发展打开了新的希望。

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  • 作者

    John J. Perona; Javin P. Oza;

  • 作者单位

    Department of Chemistry and Biochemistry,University of California, Santa Barbara, CA 93106-9510,Interdepartmental Program in Biomolecular Science and Engineering,University of California, Santa Barbara, CA 93106-9510;

    Interdepartmental Program in Biomolecular Science and Engineering,University of California, Santa Barbara, CA 93106-9510;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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  • 正文语种 eng
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