Nucleic Acids Research, Vol 25, Issue 16 3345-3353, Copyright © 1997 by Oxford University Press
C Benyajati, L Mueller, N Xu, M Pappano, J Gao, M Mosammaparast, D Conklin, H Granok, C Craig and S Elgin
The GAGA transcription factor of Drosophila melanogaster is ubiquitous and
plays multiple roles. Characterization of cDNA clones and detection by
domain- specific antibodies has revealed that the 70-90 kDa major GAGA
species are encoded by two open reading frames producing GAGA factor
proteins of 519 amino acids (GAGA-519) and 581 amino acids (GAGA- 581),
which share a common N-terminal region that is linked to two different
glutamine-rich C-termini. Purified recombinant GAGA-519 and GAGA-581
proteins can form homomeric complexes that bind specifically to a single
GAGA sequence in vitro. The two GAGA isoforms also function similarly in
transient transactivation assays in tissue culture cells and in chromatin
remodeling experiments in vitro . Only GAGA-519 protein accumulates during
the first 6 h of embryogenesis. Thereafter, both GAGA proteins are present
in nearly equal amounts throughout development; in larval salivary gland
nuclei they colocalize completely to specific regions along the euchromatic
arms of the polytene chromosomes. Coimmunoprecipitation of GAGA-519 and
GAGA-581 from crude nuclear extracts and from mixtures of purified
recombinant proteins, indicates direct interactions. We suggest that
homomeric complexes of GAGA-519 may function during early embryogenesis;
both homomeric and heteromeric complexes of GAGA-519 and GAGA-581 may
function later.
ARTICLES
Multiple isoforms of GAGA factor, a critical component of chromatin structure
Department of Biology, University of Rochester, Rochester, NY 14627, USA. tip@cb.biology.rochester.edu
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