temporary living quarters specially built by the army for soldiers; "wherever he went in the camp the men were grumbling" (同)encampment, cantonment, bivouac
shelter for persons displaced by war or political oppression or for religious beliefs (同)refugee camp
a site where care and activities are provided for children during the summer months; "city kids get to see the country at a summer camp" (同)summer camp
a penal institution (often for forced labor); "China has many camps for political prisoners"
temporary lodgings in the country for travelers or vacationers; "level ground is best for parking and camp areas"
a group of people living together in a camp; "the whole camp laughed at his mistake"
something that is considered amusing not because of its originality but because of its unoriginality; "the living room was pure camp"
establish or set up a camp (同)camp down
providing sophisticated amusement by virtue of having artificially (and vulgarly) mannered or banal or sentimental qualities; "they played up the silliness of their roles for camp effect"; "campy Hollywood musicals of the 1940s" (同)campy
live in or as if in a tent; "Can we go camping again this summer?"; "The circus tented near the town"; "The houseguests had to camp in the living room" (同)encamp, camp out, bivouac, tent
a cellular structure that is postulated to exist in order to mediate between a chemical agent that acts on nervous tissue and the physiological response
Structure of the E. coli Cyclic AMP Receptor Protein.
Identifiers
Symbol
CRP
Alt. symbols
CAP
Entrez
947867
PDB
1I5Z
RefSeq
NP_417816.1
UniProt
P0ACJ8
cAMP receptor protein (CRP; also known as catabolite activator protein, CAP) is a regulatory protein in bacteria. CRP protein binds 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, cyclic AMP receptor protein (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]
References
^ abcdefBusby S., Ebright RH. (1999). "Transcription activation by catabolite activator protein (CAP)". J. Mol. Biol. 293 (2): 199–213. doi:10.1006/jmbi.1999.3161. PMID 10550204.
^Weickert MJ, Adhya S (1993). "The galactose regulon of Escherichia coli". Mol. Microbiol. 10 (2): 245–51. doi:10.1111/j.1365-2958.1993.tb01950.x. PMID 7934815.
^Bott M (1997). "Anaerobic citrate metabolism and its regulation in enterobacteria". Arch. Microbiol. 167 (2–3): 78–88. doi:10.1007/s002030050419. PMID 9133329.
^Popovych, N.; Tzeng, S. -R.; Tonelli, M.; Ebright, R. H.; Kalodimos, C. G. (2009). "Structural basis for cAMP-mediated allosteric control of the catabolite activator protein". Proceedings of the National Academy of Sciences. 106 (17): 6927–6932. doi:10.1073/pnas.0900595106. PMC 2678429. PMID 19359484.
^Hudson, B. P.; Quispe, J.; Lara-Gonzalez, S.; Kim, Y.; Berman, H. M.; Arnold, E.; Ebright, R. H.; Lawson, C. L. (2009). "Three-dimensional EM structure of an intact activator-dependent transcription initiation complex". Proceedings of the National Academy of Sciences. 106 (47): 19830–19835. doi:10.1073/pnas.0908782106. PMC 2775702. PMID 19903881.
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… Sinensetin up-regulated expression of the adipogenic transcription factors peroxisome proliferator-activated receptor γ, CCAAT/enhancer-binding protein (C/EBP) α, and sterol regulatory element-binding protein 1c. … It also potentiated expression of C/EBPβ and activation of cAMP-responsive element-binding protein. … Sinensetin enhanced activation of protein kinase A and increased intracellular cAMP levels in 3T3-L1 preadipocytes. …
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