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Structure and activity of the atypical serine kinase Rio1

机译：非典型丝氨酸激酶Rio1的结构和活性

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摘要

Rio1 is the founding member of the RIO family of atypical serine kinases that are universally present in all organisms from archaea to mammals. Activity of Rio1 was shown to be absolutely essential in Saccharomyces cerevisiae for the processing of 18S ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. We determined high-resolution crystal structures of Archaeoglobus fulgidus Rio1 in the presence and absence of bound nucleotides. Crystallization of Rio1 in the presence of ATP or ADP and manganese ions demonstrated major conformational changes in the active site, compared with the uncomplexed protein. Comparisons of the structure of Rio1 with the previously determined structure of the Rio2 kinase defined the minimal RIO domain and the distinct features of the RIO subfamilies. We report here that Ser108 represents the sole autophosphorylation site of A. fulgidus Rio1 and have therefore established its putative peptide substrate. In addition, we show that a mutant enzyme that cannot be autophosphorylated can still phosphorylate an inactive form of Rio1, as well as a number of typical kinase substrates.
机译：Rio1是非典型丝氨酸激酶RIO家族的创始成员，该家族普遍存在于从古细菌到哺乳动物的所有生物中。在酿酒酵母中，Rio1的活性对于18S核糖体RNA的加工以及适当的细胞周期进程和染色体维持绝对是必不可少的。我们在存在和不存在结合核苷酸的情况下，确定了古细菌fulgidus Rio1的高分辨率晶体结构。与未复合的蛋白质相比，在ATP或ADP和锰离子存在下的Rio1结晶显示出活性部位的主要构象变化。 Rio1结构与先前确定的Rio2激酶结构的比较定义了最小的RIO结构域和RIO亚家族的独特特征。我们在这里报告说，Ser108代表A. fulgidus Rio1的唯一自磷酸化位点，因此建立了其推定的肽底物。此外，我们表明，不能被自身磷酸化的突变酶仍可以磷酸化非活性形式的Rio1，以及许多典型的激酶底物。

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