Protein interaction surface of the POU transcription factor UNC-86 selectively used in touch neurons

  • Röhrig S
  • Röckelein I
  • Donhauser R
 et al. 
  • 17

    Readers

    Mendeley users who have this article in their library.
  • 18

    Citations

    Citations of this article.

Abstract

The Caenorhabditis elegans POU protein UNC-86 specifies the HSN motor neurons, which are required for egg-laying, and six mechanosensory neurons. To investigate how UNC-86 controls neuronal specification, we characterized two unc-86 mutants that do not respond to touch but show wild-type egg-laying behavior. Residues P145 and L195, which are altered by these mutations, are located in the POU-specific domain and abolish the physical interaction of UNC-86 with the LIM homeodomain protein, MEC-3. This results in a failure to maintain mec-3 expression and in loss of expression of the mechanosensory neuron-specific gene, mec-2. unc-86-dependent expression of genes in other neurons is not impaired. We conclude that distinct residues in the POU domain of UNC-86 are involved in modulating UNC-86 activity during its specification of different neurons. A structural model of the UNC-86 POU domain, including base pairs and amino acid residues required for MEC-3 interaction, revealed that P145 and L195 are part of a hydrophobic pocket which is similar to the OCA-B-binding domain of the mammalian POU protein, Oct-1.

Author-supplied keywords

  • Caenorhabditis elegans
  • MEC-3
  • Neural specification
  • POU domain
  • UNC-86

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Sascha Röhrig

  • Inge Röckelein

  • Roland Donhauser

  • Ralf Baumeister

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free