The Drosophila teashirt homeotic protein is a DNA-binding protein and modulo, a HOM-C regulated modifier of variegation, is a likely candidate for being a direct target gene

Mech Dev. 1996 Oct;59(2):191-204. doi: 10.1016/0925-4773(96)00594-1.

Abstract

The Drosophila teashirt (tsh) gene has an homeotic function which, in combination with HOM-C genes, determines thoracic and abdominal (trunk) identities. Analysis of TSH protein distribution during embryogenesis using a specific polyclonal antibody shows that it is nuclear. The protein is present with regional modulation in several tissues within the trunk, suggesting additional tsh functions to those already studied. We identified a candidate tsh target shared with some HOM-C genes, the modifier of variegation gene modulo (mod). The TSH zinc-finger protein recognizes in vitro two specific sites within a 5' control element of the mod gene which responds in vivo to tsh activity. TSH is therefore a DNA binding protein and might directly control mod expression.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • DNA-Binding Proteins / chemistry*
  • Drosophila
  • Drosophila Proteins*
  • Ectoderm / metabolism
  • Genes, Homeobox*
  • Insect Hormones / chemistry*
  • Molecular Sequence Data
  • Repressor Proteins*
  • Restriction Mapping
  • Transcription Factors / chemistry*
  • Zinc Fingers*

Substances

  • DNA-Binding Proteins
  • Drosophila Proteins
  • Insect Hormones
  • Repressor Proteins
  • Transcription Factors
  • tsh protein, Drosophila