Drosophila Protein Z4 Possesses ZAD Dimerization Domain

Dokl Biol Sci. 2024 Oct;518(1):133-136. doi: 10.1134/S0012496624600179. Epub 2024 Aug 11.

Abstract

The transcription factor Z4 (putzig) is one of the key proteins that determine the chromatin structure in Drosophila. Z4 is found at the boundaries of bands on polytene chromosomes, and the bands are currently thought to correlate with chromatin domains. Z4 is a component of a protein complex that additionally includes Chromator and BEAF-32, and a conserved domain is necessary to occur at the N end of Z4 to ensure its interaction with the two proteins. In this study, a zinc finger-associated domain (ZAD) domain was identified in Z4. The capability of dimerization was confirmed for the domain by biochemical methods. A dimer model of the domain was obtained using AlphaFold2, and the model structure was confirmed using small-angle X-ray scattering (SAXS). The dimer structure shows a fold typical of ZAD domains.

Keywords: SAXS; ZAD; architectural C2H2 proteins; transcription factor; zinc-finger proteins.

MeSH terms

  • Animals
  • Drosophila Proteins* / chemistry
  • Drosophila Proteins* / genetics
  • Drosophila Proteins* / metabolism
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / metabolism
  • Protein Domains
  • Protein Multimerization*
  • Transcription Factors* / chemistry
  • Transcription Factors* / genetics
  • Transcription Factors* / metabolism

Substances

  • Drosophila Proteins
  • Transcription Factors