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Updated: Jul 13, 2026

Medium-scale Preparation of Drosophila Embryo Extracts for Proteomic Experiments
Published on: May 30, 2017
Functional studies of the BTB domain in the Drosophila GAGA and Mod(mdg4) proteins
D Read1, M J Butte, A F Dernburg
1Department of Biochemistry and Biophysics and Graduate Group in Biophysics, University of California, San Francisco, CA 94143, USA.
Abstract:
The BTB/POZ (BTB) domain is an approximately 120 residue sequence that is conserved at the N-terminus of many proteins in both vertebrates and invertebrates. We found that the protein encoded by a lethal allele of the Drosophila modifier of mdg4 [mod(mdg4)] gene has two mutated residues in its BTB domain. The identities of the residues at the positions of these mutations are highly conserved in the BTB domain family of proteins, and when the corresponding mutations were engineered into the BTB domain-containing GAGA protein, the activity of GAGA as a transcription activator in a transient transfection assay was severely reduced. The functional equivalence of the BTB domains was established by showing that the BTB domain of the mod(mdg4) protein can effectively substitute for that of GAGA.

