The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila

Erik D. Andrulis (), Janis Werner, Arpi Nazarian, Hediye Erdjument-Bromage, Paul Tempst and John T. Lis ()
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Erik D. Andrulis: Cornell University
Janis Werner: Cornell University
Arpi Nazarian: Molecular Biology Program, Memorial Sloan-Kettering Cancer Center
Hediye Erdjument-Bromage: Molecular Biology Program, Memorial Sloan-Kettering Cancer Center
Paul Tempst: Molecular Biology Program, Memorial Sloan-Kettering Cancer Center
John T. Lis: Cornell University

Nature, 2002, vol. 420, issue 6917, 837-841

Abstract: Abstract The RNA polymerase II elongation complex contains several factors that facilitate transcription elongation and catalyse the processing of precursor messenger RNAs (pre-mRNAs)1,2,3. The conserved elongation factor Spt6 is recruited rapidly and robustly to sites of active transcription4,5. Here we show that Drosophila Spt6 (dSpt6) co-purifies with the exosome, a complex of 3′ to 5′ exoribonucleases that is implicated in the processing of structural RNA and in the degradation of improperly processed pre-mRNA6,7,8,9,10. Immunoprecipitation assays of Drosophila nuclear extracts show that the exosome also associates with the elongation factor dSpt5 and RNA polymerase II. In vivo, exosome subunits colocalize with dSpt6 at transcriptionally active loci on polytene chromosomes during normal development and are strongly recruited to heat-shock loci on gene induction. At higher resolution, chromatin immunoprecipitation analysis shows that the exosome is recruited to transcriptionally active units of heat-shock genes. These data provide a physical basis for the hypothesis that exosome-mediated pre-mRNA surveillance accompanies transcription elongation.

Date: 2002
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DOI: 10.1038/nature01181

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