T4 phage-coded deoxycytidylate hydroxymethylase: Purification and studies on intermolecular interactions

Abstract

DNA precursor biosynthesis in T4 coliphage-infected bacteria is catalyzed by a complex of virus-coded enzymes, with some host cell components. As one way to explore the nature of this complex, we are purifying its constituent enzymes, so as to attempt partial or complete reconstitution of the complex. This communication describes purification to homogeneity of one of these enzymes, deoxycytidylate hydroxymethylase. The enzyme has a molecular weight of about 60,000 and consists of two subunits of identical molecular weight. Two approaches are described for studying intermolecular interactions involving this enzyme protein.