CRP interacts with promoter-bound sigma54 RNA polymerase and blocks transcriptional activation of the dctA promoter

The EMBO Journal
Y K WangH Buc

Abstract

The cAMP receptor protein (CRP) is an activator of sigma70-dependent transcription. Analysis of the sigma54-dependent dctA promoter reveals a novel negative regulatory function for CRP. CRP can bind to two distant sites of the dctA promoter, sites which overlap the upstream activator sequences for the DctD activator. CRP interacts with Esigma54 bound at the dctA promoter via DNA loop formation. When the CRP-binding sites are deleted, CRP still interacts in a cAMP-dependent manner with the stable Esigma54 closed complex via protein-protein contacts. CRP is able to repress activation of the dctA promoter, even in the absence of specific CRP-binding sites. CRP affects both the final level and the kinetics of activation. The establishment of the repression and its release by the NtrC activator proceed via slow processes. The kinetics suggest that CRP favours a new form of closed complex which interconverts slowly with the classical closed intermediate. Only the latter is capable of interacting with an activator to form an open promoter complex. Thus, Esigma54 promoters are responsive to CRP, a protein unrelated to sigma54 activators, and the repression exerted is the direct result of an interaction between Esigma54 and the CRP-cAMP...Continue Reading

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Citations

Jul 14, 2000·Journal of Bacteriology·M BuckJ D Gralla
May 11, 2002·Journal of Bacteriology·Alexandros K Kiupakis, Larry Reitzer
Aug 31, 2012·Microbiology and Molecular Biology Reviews : MMBR·Matthew Bush, Ray Dixon
Nov 9, 2010·FEMS Microbiology Reviews·Victoria Shingler
May 22, 2016·Applied and Environmental Microbiology·Ana Isabel PlateroFernando Govantes
May 26, 2010·FEMS Microbiology Letters·Fernando GovantesEduardo Santero
May 13, 1999·Journal of Bacteriology·F Rojo

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