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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-12

AUTHORS

Erik D. Andrulis, Janis Werner, Arpi Nazarian, Hediye Erdjument-Bromage, Paul Tempst, John T. Lis

ABSTRACT

The RNA polymerase II elongation complex contains several factors that facilitate transcription elongation and catalyse the processing of precursor messenger RNAs (pre-mRNAs). The conserved elongation factor Spt6 is recruited rapidly and robustly to sites of active transcription. 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-mRNA. 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. More... »

PAGES

837

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature01181

DOI

http://dx.doi.org/10.1038/nature01181

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029114035

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12490954


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50 schema:description The RNA polymerase II elongation complex contains several factors that facilitate transcription elongation and catalyse the processing of precursor messenger RNAs (pre-mRNAs). The conserved elongation factor Spt6 is recruited rapidly and robustly to sites of active transcription. 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-mRNA. 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.
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