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

Authors: Andrulis, E. D.; Werner, J.; Nazarian, A.; Erdjument-Bromage, H.; Tempst, P.; Lis, J. T.
Article Title: The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila
Abstract: The RNA polymerase II elongation complex contains several factors that facilitate transcription elongation and catalyse the processing of precursor messenger RNAs (pre-mRNAs)1-3. 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-mRNA6-10. 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.
Keywords: protein expression; nonhuman; animals; chromosomal proteins, non-histone; genes; cell line; protein binding; drosophila; transcription, genetic; nuclear proteins; rna; gene expression regulation; enzyme analysis; drosophila melanogaster; gene induction; catalysis; protein subunits; rna processing; drosophila proteins; rna polymerase ii; rna precursors; assays; rna processing, post-transcriptional; macromolecular substances; messenger rna precursor; transcriptional elongation factors; rna degradation; degradation; genes, insect; heat-shock proteins; polymerase; chromatography; exoribonuclease; exoribonucleases; precipitin tests; peptide elongation factors; priority journal; article
Journal Title: Nature
Volume: 420
Issue: 6917
ISSN: 0028-0836
Publisher: Nature Publishing Group  
Date Published: 2002-12-19
Start Page: 837
End Page: 841
Language: English
DOI: 10.1038/nature01181
PUBMED: 12490954
PROVIDER: scopus
Notes: Export Date: 14 November 2014 -- Source: Scopus
Citation Impact
MSK Authors
  1. Paul J Tempst
    324 Tempst