TAILIEUCHUNG - Báo cáo khoa học: Structure and activity of the atypical serine kinase Rio1

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 inSaccharomyces cerevisiaefor the processing of 18S ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. We determined high-resolution crystal structures ofArchaeoglobus fulgidusRio1 in the presence and absence of bound nucleotides. | iFEBS Journal Structure and activity of the atypical serine kinase Riol Nicole LaRonde-LeBlanc1 Tad Guszczynski2 Terry Copeland2 and Alexander Wlodawer1 1 Protein Structure Section Macromolecular Crystallography Laboratory NationalCancer Institute NCI-Frederick MD USA 2 Laboratory of Protein Dynamics and Signaling NationalCancer Institute NCI-Frederick MD USA Keywords autophosphorylation nucleotide complex protein kinase ribosome biogenesis Rio1 Correspondence A. Wlodawer NationalCancer Institute MCL Bldg. 536 Rm. 5 Frederick MD 21702 1201 USA Fax 1 301 8466322 Tel 1 301 8465036 E-mail wlodawer@ Received 21 April2005 revised 24 May 2005 accepted 27 May 2005 doi Riol 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. Ribosome biogenesis is fundamental to cell growth and proliferation and thereby to tumorigenesis. It has been shown that ribosome .

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