Cryo-EM reveals active site coordination within a multienzyme pre-rRNA processing complex
作者： Monica C. Pillon , Allen L. Hsu , Juno M. Krahn , Jason G. Williams , Kevin H. Goslen
DOI: 10.1038/S41594-019-0289-8
关键词: Biochemistry 、 Nuclease 、 Ribosome 、 RNA 、 Ribosomal RNA 、 Chemistry 、 Endoribonuclease 、 Ribosome assembly 、 RNase P 、 RRNA processing
摘要: Ribosome assembly is a complex process reliant on the coordination of trans-acting enzymes to produce functional ribosomal subunits and secure translational capacity cells. The endoribonuclease (RNase) Las1 polynucleotide kinase (PNK) Grc3 assemble into multienzyme complex, herein designated RNase PNK, orchestrate processing precursor RNA (rRNA). PNK belongs functionally diverse HEPN nuclease superfamily, whose members rely distinct cues for activation. To establish how coordinates its dual enzymatic activities, we solved series cryo-EM structures Chaetomium thermophilum in multiple conformational states. reveal that adopts butterfly-like architecture, harboring composite active site flanked by discrete sites. We identify two molecular switches coordinate function. Together, our corresponding studies new mechanism activation essential ribosome production.
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