Rifampicin and streptolydigin are antibiotics which inhibit prokaryotic RNA polymerase at the initiation and elongation steps, respectively. In Escherichia coli, resistance to each antibiotic results from alterations in the subunit of the core enzyme. However, in Bacillus subtilis, reconstitution studies found rifampicin resistance (Rif) associated with the subunit and streptolydigin resistance (Stl) with `. To understand the basis of bacterial Stl, we isolated the B. subtilis rpoC gene, which encodes a 1,199-residue product that is 53% identical to E. coli `. Two spontaneous Stl mutants carried the same D796G substitution in rpoC, and this substitution alone was sufficient to confer Stlin vivo. D796 falls within Region F, which is conserved among the largest subunits of prokaryotic and eukaryotic RNA polymerases. Among eukaryotes, alterations in Region F promote resistance to -amanitin, a toxin which inhibits transcription elongation; among prokaryotes, alterations in Region F cause aberrant termination. To determine whether alterations in the subunit of B. subtilis could also confer Stl, we made three Stl substitutions (A499V, G500R, and E502V) in the rif region of rpoB. Together these results suggest that and ` interact to form an Stl binding site, and that this site is important for transcription elongation.

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