Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain
Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain
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DOI：
10.1073/pnas.0604731103
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发表时间：
2006-08-08
影响因子：
11.1
通讯作者：
Brodersen, Ditlev E.
中科院分区：
文献类型：
--
作者：
Midtgaard, Soren F.;Assenholt, Jannie;Brodersen, Ditlev E.
多亚基真核外泌体是一种重要的RNA加工和降解机器。在其核形式中，外泌体与辅助因子Rrp 6p结合，其参与RNA加工和降解反应。酿酒酵母Rrp 6p的晶体结构显示了一个保守的RNase D核心，其侧翼为HRDC（解旋酶和RNase D C-末端）结构域，其构象不寻常，对酶的加工功能很重要。与AMP和UMP的复合物，RNA降解过程的产物，揭示了蛋白质如何特异性地识别核糖核苷酸及其碱基。最后，在体内突变研究表明的重要性的域接触的处理功能的Rrp 6p和突出的蛋白质和其原核核糖核酸酶D对应物之间的根本差异。
The multisubunit eukaryotic exosome is an essential RNA processing and degradation machine. In its nuclear form, the exosome associates with the auxiliary factor Rrp6p, which participates in both RNA processing and degradation reactions. The crystal structure of Saccharomyces cerevisiae Rrp6p displays a conserved RNase D core with a flanking HRDC (helicase and RNase D C-terminal) domain in an unusual conformation shown to be important for the processing function of the enzyme. Complexes with AMP and UMP, the products of the RNA degradation process, reveal how the protein specifically recognizes ribonucleotides and their bases. Finally, in vivo mutational studies show the importance of the domain contacts for the processing function of Rrp6p and highlight fundamental differences between the protein and its prokaryotic RNase D counterparts.