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Updated: May 31, 2026

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
Published on: January 16, 2017
Rrp6, rrp47 and cofactors of the nuclear exosome
J Scott Butler1, Phil Mitchell
1Departments of Microbiology and Immunology, and Biochemistry and Biophysics, and Center for RNA Biology: from Genome to Medicine, University of Rochester Medical Center, Rochester, New York, USA, scott_butler@urmc.rochester.edu.
Abstract:
This chapter reviews the present state of knowledge on the activity of enzymes that function with the RNA exosome in the nucleus. In this compartment, the exosome interacts physically and functionally with the exoribonuclease Rrp6 and several cofactors, most prominently Rrp47 and the TRAMP complex. These interactions decide the fate of RNA precursors from transcription through the formation of mature ribonucleoprotein particles (RNPs) and the export of the RNPs to the cytoplasm. The nuclear exosome catalyzes the formation of the mature 3' ends of many of these RNAs, but in other cases degrades the RNAs to mononucleotides. Cofactors such as Mpp6, TRAMP and the Nrd1/Nab3 complex play important roles in determining the outcome of the interaction of RNPs with the nuclear exosome. The details that govern the specificity of these decisions remain a rich source for future investigation.
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