CAMP receptor protein explained

CAMP receptor protein
Symbol:CRP
Altsymbols:CAP
Entrezgene:947867
Refseq:NP_417816.1
Uniprot:P0ACJ8
Pdb:1I5Z

cAMP receptor protein (CRP; also known as catabolite activator protein, CAP) is a regulatory protein in bacteria.

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.[1] [2] CRP then activates transcription through direct protein–protein interactions with RNA polymerase.[1] [2]

The genes regulated by CRP are mostly involved in energy metabolism, such as galactose, citrate, or the PEP group translocation system.[3] [4] 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.[5]

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.[1] [2] [6] At "Class II" CRP-dependent promoters, CRP binds to a DNA site that overlaps the promoter -35 element and activates transcription through two sets of protein–protein interactions: (1) an interaction between "activating region 1" of CRP and the C-terminal domain of RNA polymerase alpha subunit, and (2) an interaction between "activating region 2" of CRP and the N-terminal domain of RNA polymerase alpha subunit.[1] [2] At "Class III" CRP-dependent promoters, CRP functions together with one or more "co-activator" proteins.[1] [2]

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.[1]

Notes and References

  1. Busby S., Ebright RH. . Transcription activation by catabolite activator protein (CAP) . J. Mol. Biol. . 293 . 199–213 . 1999 . 10550204 . 10.1006/jmbi.1999.3161 . 2.
  2. Lawson CL, Swigon D, Murakami KS, Darst SA, Berman HM, Ebright RH . Catabolite activator protein: DNA binding and transcription activation . Curr. Opin. Struct. Biol. . 14 . 10–20 . 2004 . 15102444 . 10.1016/j.sbi.2004.01.012 . 1 . 2765107.
  3. Weickert MJ, Adhya S . The galactose regulon of Escherichia coli . Mol. Microbiol. . 10 . 2 . 245–51 . 1993 . 7934815 . 10.1111/j.1365-2958.1993.tb01950.x. 6872903 .
  4. Bott M . Anaerobic citrate metabolism and its regulation in enterobacteria . Arch. Microbiol. . 167 . 2–3 . 78–88 . 1997 . 9133329 . 10.1007/s002030050419. 22913073 .
  5. Popovych . N. . Tzeng . S. -R. . Tonelli . M. . Ebright . R. H. . Kalodimos . C. G. . Structural basis for cAMP-mediated allosteric control of the catabolite activator protein . 10.1073/pnas.0900595106 . Proceedings of the National Academy of Sciences . 106 . 17 . 6927–6932 . 2009 . 19359484 . 2678429 . free .
  6. Hudson . B. P. . Quispe . J. . Lara-Gonzalez . S. . Kim . Y. . Berman . H. M. . Arnold . E. . Ebright . R. H. . Lawson . C. L. . 10.1073/pnas.0908782106 . Three-dimensional EM structure of an intact activator-dependent transcription initiation complex . Proceedings of the National Academy of Sciences . 106 . 47 . 19830–19835 . 2009 . 19903881 . 2775702 . free .