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Nucleic Acids Research, 2000, Vol. 28, No. 20 3864-3870
© 2000 Oxford University Press

Functional studies of the BTB domain in the Drosophila GAGA and Mod(mdg4) proteins

Doug Read, Manish J. Butte1, Abby F. Dernburg, Manfred Frasch2 and Thomas B. Kornberg*

Department of Biochemistry and Biophysics and 1Graduate Group in Biophysics, University of California, San Francisco, CA 94143, USA and 2Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York, NY 10029, USA

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.

* To whom correspondence should be addressed. Tel: +1 415 476 8821; Fax: +1 415 514 1470; Email: tkornberg@biochem.ucsf.edu Present addresses: Doug Read, Amersham/Pharmacia Biotech, 654 Minnesota Street, San Francisco, CA 94107, USA Abby F. Dernburg, Department of Developmental Biology, Stanford University, Stanford, CA 94305, USA


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