Originally Published In
Benyajati C, Mueller L, Xu N, et al. Multiple isoforms of GAGA factor, a critical component of chromatin structure. Nucleic Acids Res. 1997;25(16):3345–3353. doi:10.1093/nar/25.16.3345
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.
Benyajati, C; Mueller, L; Xu, N; Pappano, M; Gao, J; Mosammaparast, M; Conklin, D; Granok, H; Craig, C; and Elgin, Sarah C.R., "Multiple isoforms of GAGA factor, a critical component of chromatin structure" (1997). Biology Faculty Publications & Presentations. 211.
© 1997 Oxford University Press