Yeast autonomously replicating sequence binding factor I (ABF-I) is a multifunctional phosphoprotein which plays a role in DNA replication and transcription. We fused two different portion of yeast ABFI gene to the ${eta}-Galactosidase$ gene and expressed the fusion proteins in E. coli cells. Two kinds of fusion proteins, ABFI(55-104)-lacZ and ABFI(55-367)-lacZ were produced under the control of E. coli tac promoter at a level of 35~40% and 10~15%, respectively, of total bacterial proteins. The fusion proteins retained the ${eta}-Galactosidase$ activity. The larger fusion protein was expressed in soluble forms, while the smaller fusion protein was expressed in an 80% soluble form. The two fusion proteins were purified by ${eta}-Galactosidase$ affinity chromatography. The fusion proteins contained the zinc finger motif derived from ABF-I protein but did not bind to the ABF I binding site of ARS1. The results imply a possibility that if the zinc finger motif serves as DNA binding motif, other additional regions may be required for ABF I to bind to its recognition sequence.