Abstract
Infection with bacteriophage T4 leads to a fast attachment of ADP-ribosyl residues to all subunits of DNA-dependent RNA polymerase of E. coli (Rohrer et al., 1975). This reaction termed alteration proceeds independent of protein synthesis since the ADP-ribosyl transferase is injected into the cell by the phage (Horvitz, 1974a; Rohrer et al., 1975). This enzyme uses NAD+ as substrate and affects in vivo up to 50% of the α-subunits of the RNA polymerase of E. coli under conditions of inhibited protein synthesis (Seifert et al., 1971). It is an open question whether RNA polymerase is the main target of this NAD+:protein ADP-ribosyl-transferase. How the enzymatic behavior of altered RNA polymerase or of single subunits differs from normal RNA polymerase and its subunits has to be analyzed (normal RNA polymerase= EN = β’; βαN2δ). If during phage infection protein synthesis is allowed, alteration of the subunits β’; β and δ is reverted (Horvitz, 1974a).
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Mailhammer, R. et al. (1976). RNA Polymerase Modifications after T-Phage Infections of E. coli . In: Shaltiel, S. (eds) Metabolic Interconversion of Enzymes 1975. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-66461-8_21
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DOI: https://doi.org/10.1007/978-3-642-66461-8_21
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