title: [The nature of a covalent bond between the relaxation protein and ColE1-DNA in the relaxation complex].
abstract: 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.
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004264:DNA Topoisomerases, Type I / Q000032:analysis*; D004269:DNA, Bacterial / Q000032:analysis*; D004278:DNA, Superhelical / Q000032:analysis*; D004926:Escherichia coli; D010957:Plasmids
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004278:DNA, Superhelical; D004264:DNA Topoisomerases, Type I
vernacular_title: Priroda kovalentnoĭ sviazi relaksiruiushchego belka i ColE1-DNK v relaksatsionnom komplekse.