The inducible elongin A elongation activation domain: Structure, function and interaction with the elongin BC complex

Teijiro Aso, Dewan Haque, Robert J. Barstead, Ronald C. Conaway, Joan Weliky Conaway

Research output: Contribution to journalArticlepeer-review

89 Scopus citations

Abstract

The elongin (SIII) complex strongly stimulates the rate of elongation by RNA polymerase II by suppressing transient pausing by polymerase at many sites along the DNA. Elongin (SIII) is composed of a transcriptionally active A subunit and two small regulatory B and C subunits, which bind stably to each other to form a binary complex that interacts with elongin A and strongly induces its transcriptional activity. The elongin (SIII) complex is a potential target for negative regulation by the von Hippel-Lindau (VHL) tumor suppressor protein, which is capable of binding stably to the elongin BC complex and preventing it from activating elongin A. Here, we identify an elongin A domain sufficient for activation of elongation and demonstrate that it is a novel type of inducible activator that targets the RNA polymerase II elongation complex and is evolutionarily conserved in species as distantly related as Caenorhabditis elegans and man. In addition, we demonstrate that both the elongin A elongation activation domain and the VHL tumor suppressor protein interact with the elongin BC complex through a conserved elongin BC binding site motif that is essential for induction of elongin A activity by elongin BC and for tumor suppression by the VHL protein.

Original languageEnglish (US)
Pages (from-to)5557-5566
Number of pages10
JournalEMBO Journal
Volume15
Issue number20
DOIs
StatePublished - Oct 15 1996
Externally publishedYes

Keywords

  • Elongation activation domain
  • Elongin
  • RNA polymerase II
  • Von Hippel-Lindau tumor suppressor protein

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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