Multimeric assembly and biochemical characterization of the Trax - translin endonuclease complex

C3PO was originally identified in Drosophila as a complex that enhances RNA-induced silencing complex (RISC) activity. EM and X-ray crystal structures of the Drosophila C3PO complex are now presented and endoribonuclease activity characterized. Trax–translin heteromers, also known as C3PO, have been...

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Bibliographic Details
Published in:	Nature structural & molecular biology Vol. 18; no. 6; pp. 658 - 664
Main Authors:	Tuschl, Thomas, Patel, Dinshaw J, Tian, Yuan, Simanshu, Dhirendra K, Ascano, Manuel, Diaz-Avalos, Ruben, Park, Ah Young, Juranek, Stefan A, Rice, William J, Yin, Qian, Robinson, Carol V
Format:	Journal Article
Language:	English
Published:	New York Nature Publishing Group US 01-06-2011 Nature Publishing Group
Subjects:	631/337/1645 631/45/535 Animals BASIC BIOLOGICAL SCIENCES Biochemistry Biological Microscopy Biomedical and Life Sciences Carrier Proteins - chemistry Carrier Proteins - metabolism Catalytic Domain CLEAVAGE CRYSTAL STRUCTURE Crystallography, X-Ray DROSOPHILA Drosophila melanogaster - chemistry Drosophila melanogaster - enzymology Drosophila Proteins - chemistry Drosophila Proteins - metabolism ELECTRONS ENDONUCLEASES Endoribonucleases - chemistry Endoribonucleases - metabolism GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE Kinetics Life Sciences Mass Spectrometry Membrane Biology Microscopy, Electron Models, Molecular Molecular biology OCCUPANTS Protein Multimerization Protein Structure Protein Structure, Quaternary Proteins Ribonucleic acid RNA RNA - metabolism SUBSTRATES United States
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