The BTB Domain of bric à brac Mediates Dimerization In Vitro | Zendy

Wei Chen | Zendy; Susan Zollman | Zendy; JeanLouis Couderc | Zendy; Frank A. Laski | Zendy

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The BTB Domain of bric à brac Mediates Dimerization In Vitro

Author(s) -

Wei Chen,

Susan Zollman,

JeanLouis Couderc,

Frank A. Laski

Publication year - 1995

Publication title -

molecular and cellular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.14

H-Index - 327

eISSN - 1067-8824

pISSN - 0270-7306

DOI - 10.1128/mcb.15.6.3424

Subject(s) - biology , zinc finger , amino acid , drosophila melanogaster , in vitro , gene , microbiology and biotechnology , genetics , protein domain , domain (mathematical analysis) , melanogaster , biochemistry , transcription factor , mathematical analysis , mathematics

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.

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