The BTB domain of bric à brac mediates dimerization in vitro.
The gene bric à brac (bab) is required for the proper development of the limbs and ovary in Drosophila melanogaster. bab encodes a BTB domain (also called a POZ domain), an approximately 115-amino-acid conserved motif found primarily in the N termini of zinc finger proteins. In this paper, we show that the BTB domain of bab can mediate protein dimerization in vitro. In addition, we demonstrate that the first 51 amino acids of the bab BTB domain are sufficient for dimerization, and we identify amino acids within this region that are required for binding.
Chen
W
W
Department of Biology, University of California, Los Angeles 90024, USA.
Zollman
S
S
Couderc
J L
JL
Laski
F A
FA
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004268:DNA-Binding Proteins / Q000737:chemistry*; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000235:genetics* / Q000254:growth & development; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D017510:Protein Folding; D016415:Sequence Alignment; D014157:Transcription Factors / Q000737:chemistry*; D016335:Zinc Fingers
C093752:Bric-a-brac protein 1, Drosophila; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D014157:Transcription Factors