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

  title={The inducible elongin A elongation activation domain: structure, function and interaction with the elongin BC complex.},
  author={Teijiro Aso and Dewan Haque and Robert J. Barstead and Ronald C. Conaway and Joan W. Conaway},
  journal={The EMBO Journal},
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… 

Identification and Characterization of Elongin A2, a New Member of the Elongin Family of Transcription Elongation Factors, Specifically Expressed in the Testis*

Cl cloning, expression, and characterization of human Elongin A2 are reported on, a novel transcription elongation factor that exhibited 47% identity and 61% similarity to ElongIn A.

Identification and Biochemical Characterization of a Novel Transcription Elongation Factor, Elongin A3*

The molecular cloning, expression, and biochemical characterization of human Elongin A3, a novel transcription elongation factor that exhibits 49 and 81% identity to Elongsin A and the recently identified ElongIn A2, respectively are reported on.

Identification of Elongin C Sequences Required for Interaction with the von Hippel-Lindau Tumor Suppressor Protein*

The finding that only a subset of Elongin C sequences required for its interaction with Elong in A are critical for binding to VHL may offer the opportunity to develop reagents that selectively interfere with Elongsin and VHL function.

In Vivo Requirement of the RNA Polymerase II Elongation Factor Elongin A for Proper Gene Expression and Development

RNA interference-mediated depletion of dEloA demonstrated that elongin A is an essential factor that is required for proper metamorphosis and defined the novel contribution played by RNA polymerase II elongation machinery in regulation of gene expression that is necessary for proper development.

Functional characterization of a mammalian transcription factor, Elongin A.

Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Lindau peptide.

Elongin is a transcription elongation factor that stimulates the rate of elongation by suppressing transient pausing by RNA polymerase II at many sites along the DNA. It is heterotrimeric in mammals,

Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C.

  • M. BotuyanC. Koth W. Chazin
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1999
Yeast elongin C is found to oligomerize in solution and to undergo significant structural rearrangements upon binding of two different partner proteins, suggesting a structural basis for the interaction of an F-box-containing protein with a SKP1 homologue and the modulation of this interaction by the tumor suppressor VHL.

Transcriptional Properties of Mammalian Elongin A and Its Role in Stress Response*

Evidence is presented that Elongin A associates with the IIO form of RNAPII at sites of newly transcribed RNA and is relocated to dotlike domains distinct from those containingRNAPII when cells are treated with the kinase inhibitor 5,6-dichloro-1-β-d-ribofuranosylbenzimidazole.

Mammalian Elongin A complex mediates DNA‐damage‐induced ubiquitylation and degradation of Rpb1

The results suggest that mammalian Elongin A is directly involved in ubiquitylation and degradation of Rpb1 following DNA damage.


Program Manualfor the GCG Package, Version 8

  • Genetics Computer Group
  • 1994