cAMPCRP

cAMPCRP refers to the complex formed by cyclic AMP (cAMP) and the cAMP receptor protein (CRP), a widely studied transcriptional regulator in many bacteria. In Escherichia coli and related species, the CRP–cAMP complex is often called CAP (catabolite activator protein). The complex acts as a global regulator that coordinates the use of available carbon sources.

Mechanism and DNA binding: CRP is a homodimer. When each monomer binds one molecule of cAMP, a conformational change enables high-affinity DNA binding. The CRP–cAMP dimer recognizes a palindromic DNA motif about 22 base pairs long, typically upstream of promoters. Binding of the complex facilitates recruitment or stabilization of RNA polymerase at certain promoters, primarily activating transcription (Class I and Class II promoters); in other contexts, it can repress transcription through competitive or cooperative interactions with other regulators.

Structure and regulation: Each CRP monomer (~210 amino acids) contains an N-terminal cAMP-binding domain and a C-terminal DNA-binding domain featuring a helix-turn-helix motif. cAMP binding induces structural rearrangements that align the DNA-binding domains for operator contact. Regulation is linked to cellular energy status: cAMP levels rise when glucose is scarce due to adenylate cyclase activity, and decrease when glucose is abundant, thereby modulating CRP–cAMP–dependent transcription.

Biological significance: The CRP–cAMP system integrates carbon source availability with global gene expression, controlling operons such as lac, gal, ara, and others involved in carbohydrate utilization. It is a model example of allosteric regulation in transcriptional control and has been leveraged in metabolic engineering and functional genomics. Variations exist across species, but the general cAMPCRP mechanism is widely conserved in bacteria.