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Site crp
- Name: crp
- Type: Gene
- Synonyms
b3357 MG1655 locus tag cap csm - Mnemonic: cAMP receptor protein
- Left End Point: 75.09
- Right End Point: 75.11
- Products:
cyclic AMP receptor protein CAP, catabolite activator protein - Direction: >
- Properties:
Property Comment autogenously regulated NULL - Priority: 1
- 8 Alleles of This Gene
crp-1 crp-1004 crp-120 crp-2 crp-3(del) crp-39(del) crp-45(del) crp-765(del)::kan - External Database Links:
Host Site Page Links NCBI/GenBank J01598 EcoGene.org EG10164 EcoliWiki crp - Comment:
- Sel. Pheno. Loss: phage lambda + nalidixic acid res.; strep. + cAMP res.; phage lambda res. on arabin. + maltose indic.plates glucose 6-phos. + cAMP res. or D-xylose + L-arab.+gluc. 6-phos. + cAMP res
- References:
- Thirion, J.P., M. Hofnung 1972. On some genetic aspects of phage lambda resistance in E. coli K12. Genetics 71:207-216
- Brickman, E., L. Soll, J.R. Beckwith 1973. Genetic characterization of mutations which affect catabolite-sensitive operons in Escherichia coli, including deletions of the gene for adenyl cyclase. J.Bacteriol. 116:582-587
- Beacham, I.R., R. Kahana, L. Levy, E. Yagil 1973. Mutants of Escherichia coli K-12 "cryptic" or deficient in 5'-nucleotidase (uridine diphosphate-sugar hydrolase) and 3'-nucleotidase (cyclic phosphodiesterase) activity. J.Bacteriol. 116:957-964
- Ackerman, R.S., N.R. Cozzarelli, W. Epstein 1974. Accumulation of toxic concentrations of methylglyoxal by wild-type Escherichia coli K-12. J.Bacteriol. 119:357-362
- Kumar, A., V.F. Maples, W.S. Champney 1976. Properties of adenyl cyclase and cyclic adenosine 3',5'-monophosphate receptor protein-deficient mutants of Escherichia coli. J.Bacteriol. 125:545-555
- Artman, M., S. Werthamer 1979. Use of streptomycin and cyclic adenosine 5'-monophosphate in the isolation of mutants deficient in CAP protein. J.Bacteriol. 120:542-544
- Daniel, J., A. Danchin 1979. Involvement of cyclic AMP and its receptor protein in the sensitivity of Escherichia coli K12 toward serine. Mol.Gen.Genet. 176:343-350
- Guidi-Rontani, C., A. Danchin, A. Ullmann 1981. Isolation and characterization of an Escherichia coli mutant affected in the regulation of adenylate cyclase. J.Bacteriol. 148:753-761
- Cossart, P., B. Gicquel-Sanzey 1982. Cloning and sequencing of the crp gene of Escherichia coli K12. Nucleic Acids Res. 10:1363-1378
- Aiba, H., S. Fujimoto, N. Ozaki 1982. Molecular cloning and nucleotide sequencing of the gene for E. coli cAMP receptor protein. Nucleic Acids Res. 10:1345-1361
- George, S.E., T. Melton 1986. Cloning and molecular characterization of csm mutations allowing expression of catabolite-repressible operons in the absence of exogenous cyclic AMP. J.Bacteriol. 166:533-540
- Smirnov, Y.V., A.F. Lisenkov 1986. Construction of the hybrid crp-lac operon and investigation of the role of the CRP-cAMP complex in its regulation in Escherichia coli. Soviet Genet. 22:432-438
- Okamoto, K., M. Freundlich 1986. Mechanism for the autogenous control of the crp operon: transcriptional inhibition by a divergent RNA transcript. Proc.Natl.Acad.Sci.USA 83:5000-5004
- Puyo, M.F., P. Calsou, B. Salles 1992. UV resistance of E. coli K-12 deficient in cAMP/CRP regulation. Mutat.Res. 282:247-252
- Rasmussen, P.B., B. Holst, P. Valentin-Hansen 1996. Dual-function regulators: the cAMP receptor protein and the CytR regulator can act either to repress or to activate transcription depending on the context. Proc.Natl.Acad.Sci.USA 93:10151-10155
- Kimata, K., H. Takahashi, T. Inada, P. Postma, H. Aiba 1997. cAMP receptor protein-cAMP plays a crucial role in glucose-lactose diauxie by activating the major glucose transporter gene in Escherichia coli. Proc.Natl.Acad.Sci.USA 94:12914-12919
- Lopata, M., D. Schlieper, B. von Wilcken-Bergmann, B. Muller-Hill 1997. A lethal mutant of the catabolite gene activator protein CAP of Escherichia coli. Biol. Chem 378:1153-1162
- Belyaeva, T.A., V.A. Rhodius, C.L. Webster, S.J. Busby 1998. Transcription activation at promoters carrying tandem DNA sites for the Escherichia coli cyclic AMP receptor protein: organisation of the RNA polymerase alpha subunits. J.Mol.Biol. 277:789-80