ADP‐Ribosylation of DNA‐Dependent RNA Polymerase of <i>Escherichia coli</i> by an NAD⁺: Protein ADP‐ribosyltransferase from Bacteriophage T4

Abstract

A protein from bacteriophage T4 responsible for the alteration of host DNA-dependent RNA polymerase and absent in T4 alt- phage was purified from T4 phage and enriched from T4-infected cells. It is injected during infection together with the known internal proteins. It has a molecular weight of about 70000 and catalyses the release of nicotinamide and the transfer of the ADP-ribosyl moiety from NAD+ to arginyl residues of various proteins including itself. RNA polymerase from Escherichia coli accepts ADP-ribosyl residues in all four subunits; the alpha subunit reacts with very high specificity. Only half of the alpha subunits are labelled, 45% with one, 5% with two residues. The main product shows the same electrophoretic mobility as alpha subunits altered or modified in vivo. The alpha subunit in modified RNA polymerase is no acceptor.