One functional subunit is sufficient for catalytic activity and substrate specificity of Escherichia coli endoribonuclease III artificial heterodimers.

To study the intersubunit communication required for the activity of the normally homodimeric enzyme endoribonuclease III of Escherichia coli we have constructed and analysed an artificial heterodimer. This heterodimer is composed of one wild-type and one catalytically inactive subunit. The inactive subunit has one amino acid exchanged (E117K, rnc70 mutant) which abolishes cleavage activity but still allows substrate binding of a rnc70-homodimer. Our results show that one functional active site is sufficient for cleavage activity of the heterodimer.