Analysis of the Saccharomyces cerevisiae exosome architecture and of the RNA binding activity of Rrp40p.
The exosome is a complex of eleven subunits in yeast, involved in RNA processing and degradation. Despite the extensive in vivo functional studies of the exosome, little information is yet available on the structure of the complex and on the RNase and RNA binding activities of the individual subunits. The current model for the exosome structure predicts the formation of a heterohexameric RNase PH ring, bound on one side by RNA binding subunits, and on the opposite side by hydrolytic RNase subunits. Here, we report protein-protein interactions within the exosome, confirming the predictions of constituents of the RNase PH ring, and show some possible interaction interfaces between the other subunits. We also show evidence that Rrp40p can bind RNA in vitro, as predicted by sequence analysis.
Luz
J S
JS
Department of Biochemistry, Institute of Chemistry, University of São Paulo, Av. Prof. Lineu Prestes 748, São Paulo, SP 05508-900, Brazil.
Tavares
J R
JR
Gonzales
F A
FA
Santos
M C T
MC
Oliveira
C C
CC
D005095:Exoribonucleases / Q000737:chemistry* / Q000378:metabolism; D063326:Exosome Multienzyme Ribonuclease Complex; D046912:Multiprotein Complexes / Q000737:chemistry*; D011485:Protein Binding; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism
D046912:Multiprotein Complexes; D016601:RNA-Binding Proteins; D029701:Saccharomyces cerevisiae Proteins; D012313:RNA; C056502:ribonuclease PH; D005095:Exoribonucleases; D063326:Exosome Multienzyme Ribonuclease Complex; C518474:Rrp40 protein, S cerevisiae