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Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex

机译：RNA结合的11亚基真核外泌体复合物的晶体结构

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摘要

负责RNA周转的主要因子是一个被称为“外来rn体”的含十个亚单元的复合物。这一复合物含rn有一个活跃的Rnase亚单元，即Rrp44。在细rn胞核中，“外来体”吸收一个辅助因子，后者rn也是一种核酸酶，即Rrp6。这项研究报告了rn个440-kilodalton的复合物的2．8 A分辨率的晶rn体结构，它由核心酵母“外来体”、Rrp6的一rn个羧基端部区域和一个RNA双链组成。该结rn构显示了RNA是怎样被识别并为降解做好准rn备的。%The exosome is the major 3'-5' RNA-degradation complex in eukaryotes. The ubiquitous core of the yeast exosome (Exo-10) is formed by nine catalytically inert subunits (Exo-9) and a single active RNase, Rrp44. In the nucleus, the Exo-10 core recruits another nuclease, Rrp6. Here we crystallized an approximately 440-kilodalton complex of Saccharomyces cerevisiae Exo-10 bound to a carboxy-terminal region of Rrp6 and to an RNA duplex with a 3'-overhang of 31 ribonucleotides. The 2.8 A resolution structure shows how RNA is funnelled into the Exo-9 channel in a single-stranded conformation by an unwinding pore. Rrp44 adopts a closed conformation and captures the RNA 3'-end that exits from the side of Exo-9. Exo-9 subunits bind RNA with sequence-unspecific interactions reminiscent of archaeal exosomes. The substrate binding and channelling mechanisms of 3'-5' RNA degradation complexes are conserved in all kingdoms of life.
机译：负责RNA周转的主要因子是一个被称为“外来rn体”的含十个亚单元的复合物。这一复合物含rn有一个活跃的Rnase亚单元，即Rrp44。在细rn胞核中，“外来体”吸收一个辅助因子，后者rn也是一种核酸酶，即Rrp6。这项研究报告了rn个440-kilodalton的复合物的2．8 A分辨率的晶rn体结构，它由核心酵母“外来体”、Rrp6的一rn个羧基端部区域和一个RNA双链组成。该结rn构显示了RNA是怎样被识别并为降解做好准rn备的。%The exosome is the major 3'-5' RNA-degradation complex in eukaryotes. The ubiquitous core of the yeast exosome (Exo-10) is formed by nine catalytically inert subunits (Exo-9) and a single active RNase, Rrp44. In the nucleus, the Exo-10 core recruits another nuclease, Rrp6. Here we crystallized an approximately 440-kilodalton complex of Saccharomyces cerevisiae Exo-10 bound to a carboxy-terminal region of Rrp6 and to an RNA duplex with a 3'-overhang of 31 ribonucleotides. The 2.8 A resolution structure shows how RNA is funnelled into the Exo-9 channel in a single-stranded conformation by an unwinding pore. Rrp44 adopts a closed conformation and captures the RNA 3'-end that exits from the side of Exo-9. Exo-9 subunits bind RNA with sequence-unspecific interactions reminiscent of archaeal exosomes. The substrate binding and channelling mechanisms of 3'-5' RNA degradation complexes are conserved in all kingdoms of life.

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  • 来源
    《Nature》 |2013年第7439期|70-75B2|共7页
  • 作者

    Debora Lika Makino; Marc Baumgartner; Elena Conti;

  • 作者单位

    Department of Structural Cell Biology, MPI for Biochemistry, Am Klopferspitz 18,82152 Martinsried, Germany;

    Department of Structural Cell Biology, MPI for Biochemistry, Am Klopferspitz 18,82152 Martinsried, Germany;

    Department of Structural Cell Biology, MPI for Biochemistry, Am Klopferspitz 18,82152 Martinsried, Germany;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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