Bacterial promoters differ in the number of RNA polymerase molecules that bind to form a
filterable polymerase-promoter complex. We show that two holoenzyme molecules interact …

Sigma factors, the key regulatory components of the bacterial RNA polymerase (RNAP),
direct promoter DNA binding and DNA melting. The σ54‐RNAP forms promoter complexes …

Control of transcription frequently involves the direct interaction of activators with RNA
polymerase. In bacteria, the formation of stable open promoter complexes by the ς 54 RNA …

A functional transcription elongation complex can be formed without passing through a
promoter by adding a complementary RNA primer and core Escherichia coli RNA …

Transcriptional activator proteins in bacteria often operate by interaction with the C-terminal
domain of the α-subunit of RNA polymerase (RNAP). Here we report the discovery of an …

Bacterial enhancer-binding proteins (EBP) activate transcription by hydrolyzing ATP to
restructure the σ54-RNA polymerase–promoter complex. We compare six high resolution …

We report experiments designed to elucidate the mechanism by which RNA polymerase
advances from the open complex to synthesis of a stably bound RNA chain during …

The bacterial σ54 protein associates with core RNA polymerase to form a holoenzyme that
functions in enhancer‐dependent transcription. Isomerization of the σ54 polymerase and its …

The bacterial σ54 RNA polymerase functions in a transcription activation mechanism that
fully relies upon nucleotide hydrolysis by an enhancer binding activator protein to stimulate …

The N-terminal domain of the RNA polymerase α subunit (α-NTD) was tested for a role in
transcription activation by a variety of AraC/XylS family members. Based on substitutions at …