Abstract
A mouse cDNA that encodes a nuclear DNA binding protein was identified by yeast two-hybrid screening using the activation domain 2 of the nuclear receptor coactivator TIF2 as a bait. BLAST analysis revealed that the identified cDNA encodes a KDWK domain and contains sequences almost identical to three tryptic peptides of rat GMEB-1 which together with the GMEB-2 heterodimeric partner binds to the GME/CRE sequence (glucocorticoid modulatory element) of the tyrosine aminotransferase (TAT) promoter. Mouse GMEB-1 is ubiquitously expressed in all the tissues examined. In vitro translated mGMEB-1 bound specifically to GME oligonucleotides, either alone or as a heterodimer with rGMEB-2. Transient transfection experiments with TAT promoter reporter genes suggest a potential role for mGMEB-1 as a transcriptional regulator of the TAT promoter.
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