ISOLATION AND CHARACTERIZATION OF A STREPTOLYDIGIN RESISTANT RNA POLYMERASE

THE RNA polymerase of Escherichia coli consists of two small subunits α, two larger subunits β and β′, and one subunit σ which aids initiation1. A question relevant to control of polymerase synthesis is whether genes coding for the various subunits are contiguous. Both rifampicin resistant RNA polymerase and streptovaricin resistant RNA polymerase map near the argH locus2,3. Here I report that (a) streptolydigin inhibits chain elongation by E. coli RNA polymerase as was found by Siddhikol et al.4 for the polymerase of B. megaterium, (b) mutants altering the polymerase to streptolydigin resistance also map near argH, and (c) that, as is the case of rifampicin resistance1,2, the core" enzyme (the α2ββ′ structure which itself possesses enzymatic activity) is modified in the resistant mutant. © 1969 Nature Publishing Group."