BEN: a novel domain in chromatin factors and DNA viral proteins

Bioinformatics. 2008 Feb 15;24(4):458-61. doi: 10.1093/bioinformatics/btn007. Epub 2008 Jan 18.

Abstract

We report a previously uncharacterized alpha-helical module, the BEN domain, in diverse animal proteins such as BANP/SMAR1, NAC1 and the Drosophila mod(mdg4) isoform C, in the chordopoxvirus virosomal protein E5R and in several proteins of polydnaviruses. Contextual analysis suggests that the BEN domain mediates protein-DNA and protein-protein interactions during chromatin organization and transcription. The presence of BEN domains in a poxviral early virosomal protein and in polydnaviral proteins also suggests a possible role for them in organization of viral DNA during replication or transcription.

Publication types

  • Research Support, N.I.H., Intramural

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chromatin / metabolism*
  • Chromosomal Proteins, Non-Histone / chemistry*
  • DNA Viruses / chemistry*
  • Drosophila Proteins / chemistry
  • Evolution, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Viral Proteins / chemistry*

Substances

  • Chromatin
  • Chromosomal Proteins, Non-Histone
  • Drosophila Proteins
  • Viral Proteins