CAMP receptor protein

Protein

CRP protein binds cyclic adenosine monophosphate (cAMP), which causes a conformational change that allows CRP to bind tightly to a specific DNA site in the promoters of the genes it controls. CRP then activates transcription through direct protein–protein interactions with RNA polymerase.

The genes regulated by CRP are mostly involved in energy metabolism, such as galactose, citrate, or the PEP group translocation system. In Escherichia coli, CRP can regulate the transcription of more than 100 genes.

The signal to activate CRP is the binding of cyclic AMP. Binding of cAMP to CRP leads to a long-distance signal transduction from the N-terminal cAMP-binding domain to the C-terminal domain of the protein, which is responsible for interaction with specific sequences of DNA.{{Cite journal | doi-access = free

At "Class I" CRP-dependent promoters, CRP binds to a DNA site located upstream of core promoter elements and activates transcription through protein–protein interactions between "activating region 1" of CRP and the C-terminal domain of RNA polymerase alpha subunit.{{Cite journal | doi-access = free

At most CRP-dependent promoters, CRP activates transcription primarily or exclusively through a "recruitment" mechanism, in which protein–protein interactions between CRP and RNA polymerase assist binding of RNA polymerase to the promoter.

References

References

1. Busby S., [[Richard H. Ebright. (1999). "Transcription activation by catabolite activator protein (CAP)". J. Mol. Biol..
2. (2004). "Catabolite activator protein: DNA binding and transcription activation". Curr. Opin. Struct. Biol..
3. (1993). "The galactose regulon of Escherichia coli". Mol. Microbiol..
4. Bott M. (1997). "Anaerobic citrate metabolism and its regulation in enterobacteria". Arch. Microbiol..
5. Fic, E.. (2008-11-25). "cAMP Receptor Protein from Escherichia coli as a Model of Signal Transduction in Proteins – A Review". Journal of Molecular Microbiology and Biotechnology.