[The nature of a covalent bond between the relaxation protein and ColE1-DNA in the relaxation complex].

O-[32P]phosphoserine was found to be the only phosphoamino acid in the acid hydrolysate of the [32P]ColE1 DNA-peptide produced by action of proteases on the ColE1 DNA relaxation complex. This finding suggests that the relaxation protein is bound to ColE1 DNA in the relaxation complex via a phosphodiester linkage between a serine hydroxyl of the protein and the 5'-phosphate of the terminal deoxycytidine residue of the DNA.