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Vol. 12, No. 19, pp. 3123-3136, October 1, 1998
factor FlgM actively dissociates Salmonella typhimurium 28 RNA polymerase holoenzyme
Department of Microbiology, University of Washington,
Seattle, Washington 98195 USA
The anti-
factor FlgM of Salmonella typhimurium inhibits
transcription of class 3 flagellar genes through a direct interaction with the flagellar-specific factor, 28. FlgM is
believed to prevent RNA polymerase (RNAP) holoenzyme formation by
sequestering free 28. We have analyzed FlgM-mediated
inhibition of 28 activity in vitro. FlgM is able to
inhibit 28 activity even when 28 is first
allowed to associate with core RNAP. Surface plasmon resonance (SPR)
was used to evaluate the interaction between FlgM and both
28 and 28 holoenzyme (E28). The
Kd of the 28-FlgM complex is
~2 × 10
10 M; missense mutations in FlgM
that cause a defect in 28 inhibition in vivo increase the
Kd of this interaction by 4- to 10-fold. SPR
measurements of E28 dissociation in the presence of FlgM
indicate that FlgM destabilizes E28, presumably via an
interaction with the subunit. Our data provide the first direct
evidence of an interaction between FlgM and E28. We
propose that this secondary activity of FlgM, which we term holoenzyme
destabilization, enhances the sensitivity of the cell to changes in
FlgM levels during flagellar biogenesis.
[Key Words:
-factors; RNA polymerase; transcription; Salmonella typhimurium]
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