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PMID: 7760839 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Retracted Publication

The BTB domain of bric à brac mediates dimerization in vitro.

Molecular and cellular biology ·Vol. 15 ·No. 6 ·1995-06-00 ·Pages 3424-9

Chen W, Zollman S, Couderc JL, Laski FA

Abstract

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.

Related Genes
BAB
MeSH Terms
Amino Acid Sequence Animals Base Sequence DNA-Binding Proteins/chemistry Drosophila Proteins Drosophila melanogaster/genetics,growth & development Molecular Sequence Data Peptide Mapping Protein Folding Sequence Alignment Transcription Factors/chemistry Zinc Fingers
Chemicals
Bric-a-brac protein 1, Drosophila DNA-Binding Proteins Drosophila Proteins Transcription Factors
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Chen W
Department of Biology, University of California, Los Angeles 90024, USA.
Zollman S
Couderc J L
Laski F A
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/MCB.15.6.3424
Published
1995-06-00
Pages
3424-9
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC230577
Subset
IM
Databases
GENBANK
L08483, L22205, U00115, U01333, U14399, X17121, X54663, X75498, X82018, Z19002, Z21943
Corrections
RetractionIn
PMID: 9380040
External Links
PubMed source DOI: 10.1128/MCB.15.6.3424 PMC Full Text View journal details
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