CTCF and Sgfl1 proteins form alternative complexes with ENY2 proteins

Dokl Biochem Biophys. 2016 May;468(1):180-2. doi: 10.1134/S1607672916030054. Epub 2016 Jul 15.

Abstract

ENY2 is a multifunctional protein, a component of the SAGA complex (protein complex involved in the regulation of transcription, possessing histone-acetyltransferase and H2B-histone-deubiquitinylating activities [1]) and TREX-2 (complex involved in the mRNA nuclear export [2]). Besides this, the interactions of ENY2 with DNA-binding insulator proteins Su(Hw) and dCTCF have been described as essential for the barrier activity of corresponding insulators [3, 4]. In this study, we described the formation of mutually exclusive complexes of ENY2 with insulator proteins and Sgfl1-a component of the SAGA complex, direct binding partner for ENY2.

MeSH terms

  • Animals
  • CCCTC-Binding Factor
  • Drosophila
  • Drosophila Proteins / metabolism*
  • Escherichia coli
  • Escherichia coli Proteins / metabolism
  • Humans
  • Molecular Docking Simulation
  • Nuclear Magnetic Resonance, Biomolecular
  • Repressor Proteins / metabolism*
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Transcription Factors / metabolism*

Substances

  • CCCTC-Binding Factor
  • CTCF protein, human
  • Drosophila Proteins
  • Escherichia coli Proteins
  • Repressor Proteins
  • SGF11 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Sgf11 protein, Drosophila
  • Transcription Factors