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Functional studies of the BTB domain in the Drosophila GAGA and Mod(mdg4) proteins NUCLEIC ACIDS RESEARCH Read, D., Butte, M. J., Dernburg, A. F., Frasch, M., Kornberg, T. B. 2000; 28 (20): 3864-3870

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.

View details for Web of Science ID 000089954300004

View details for PubMedID 11024164