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Related Experiment Videos

A functional interaction between RHA and Ubc9, an E2-like enzyme specific for Sumo-1.

Joanna Argasinska1, Kai Zhou, Robert J Donnelly

  • 1Department of Biochemistry and Molecular Biology, Graduate School of Biomedical Sciences, University of Medicine and Dentistry of New Jersey, 185 South Orange Avenue, Newark, NJ 07103, USA.

Journal of Molecular Biology
|August 18, 2004
PubMed
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Ubc9 interacts with RNA helicase A (RHA) and enhances its transcription activity, independent of Ubc9

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Protein Interactions

Background:

  • RNA helicase A (RHA), a DEAH family protein, is implicated in chromatin DNA topology, affecting transcription and chromosome condensation.
  • Ubc9, an E2 enzyme for Sumo-1, was previously found essential for RHA and topoisomerase IIalpha interaction.

Purpose of the Study:

  • To investigate the functional interaction between Ubc9 and RNA helicase A (RHA).
  • To determine Ubc9's role in regulating RHA's transcription activity.
  • To identify the domains involved in the RHA-Ubc9 interaction and the effect of Ubc9 on RHA modification.

Main Methods:

  • Investigated RHA-Ubc9 interaction using in vitro and in vivo assays.
  • Measured RHA transcription activity in a CREB-mediated pathway.

Related Experiment Videos

  • Mapped the RHA domain responsible for Ubc9 binding.
  • Assessed Sumo-1 conjugation of RHA upon Ubc9 interaction.

    • Main Results:

    • Ubc9 functionally interacts with RHA and activates its transcription activity.
    • The N-terminal domain (residues 1-137) of RHA mediates Ubc9 binding.
    • Ubc9 interaction induces Sumo-1 conjugation of RHA in vitro and in vivo.
    • Ubc9's catalytic activity is not required for RHA transcription activation.

    Conclusions:

    • Ubc9 is a novel factor that activates RHA transcription activity.
    • Ubc9 binding to RHA's N-terminus leads to RHA Sumo-1ylation.
    • Ubc9 plays multiple regulatory roles in RHA function, potentially independent of its catalytic activity.