[Isolation of mitochondrial DNA binding proteins which are specific for maize cox1 promoter]

We purified DNA binding proteins which interact with the promoter region of cox1 gene from maize mitochondria. Presence of poly[dIdC-dIdC] and KCl in concentrations up to 500 mM had no influence on binding efficiency demonstrating high specificity of complexes formed. Surprisingly, we did not detect DNA binding when probes containing promoter regions of other mitochondrial genes (cox3, rrn26) were used. Mobility shift competition studies also suggest that the protein posseses binding specificity towards cox1 promoter. The core motif AAGTA proved to be necessary for DNA binding. Using combination of EMSA and elution of proteins from PAG we showed that DNA-protein complex formed contains three polypeptides with molecular mass 60, 44 and 22 kD. We suggest that the isolated proteins may play an important role in the regulation of plant cox1 gene transcription.