Electromobility shift assays with a DNA probe containing the RPG box identified a specific DNA-binding protein in total protein extracts of The protein, named Rbf1p (RPG-box-binding protein 1), bound to other S. cerevisiae RPG boxes, although the nucleotide recognition profile was not completely the same as that of S. cerevisiae Rap1p (repressor-activator protein 1), an RPG-box-binding protein. The repetitive sequence of the chromosomal telomere also competed with RPG-box binding to Rbf1p. For further analysis, we purified Rbf1p 57600-fold from total protein extracts, raised mAbs against the purified protein and immunologically cloned the gene, whose ORF specified a protein of 527 aa. The bacterially expressed protein showed RPG-box-binding activity with the same profile as that of the purified one. The Rbf1p, containing two glutamine-rich regions that are found in many transcription factors, showed transcriptional activation capability in and was predominantly observed in nuclei. These results suggest that Rbf1p is a transcription factor with telomere-binding activity in


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