Transcription Factor
Accessions: | ECK120004636 (RegulonDB 7.5) |
Names: | CRP, CRP transcriptional dual regulator |
Organisms: | ECK12 |
Libraries: | RegulonDB 7.5 1 1 Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muniz-Rascado L, Garcia-Sotelo JS, Weiss V, Solano-Lira H, Martinez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernandez S, Alquicira-Hernandez K, Lopez-Fuentes A, Porron-Sotelo L, Huerta AM, Bonavides-Martinez C, Balderas-Martinez YI, Pannier L, Olvera M, Labastida A, Jimenez-Jacinto V, Vega-Alvarado L, Del Moral-Chavez V, Hernandez-Alvarez A, Morett E, Collado-Vides J. RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more. Nucleic Acids Res. 2013 Jan 1;41(D1):D203-D213. [Pubmed] |
Notes: | global; cytoplasm; Transcription related; repressor; zinc ion binding; regulation of transcription, DNA-dependent; cAMP binding; intracellular; sequence-specific DNA binding transcription factor activity; DNA binding; nucleotide binding; transcription, DNA-dependent; transcription activator activity; transcription repressor activity; activator |
Length: | 211 |
Pfam Domains: | 23-111 Cyclic nucleotide-binding domain 142-206 Crp-like helix-turn-helix domain 166-197 Bacterial regulatory proteins, crp family |
Sequence: (in bold interface residues) | 1 MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEM 60 61 ILSYLNQGDFIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMRLSAQ 120 121 MARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKITRQEIGQIVGCS 180 181 RETVGRILKMLEDQNLISAHGKTIVVYGTR* |
Interface Residues: | 27, 81, 166, 171, 180, 181, 182, 183, 185, 186 |
3D-footprint Homologues: | 3iyd_H, 4a12_B, 2xro_E, 5i2d_R, 3mzh_A, 7pza_B, 3e6c_C, 4i2o_B |
Binding Motifs: | CRP wtgtGAwyyasaTCACAwwwtt |
Binding Sites: | ECK120011238 ECK120011310 ECK120011316 ECK120011318 ECK120011343 ECK120011443 ECK120011446 ECK120011452 ECK120011480 ECK120011487 ECK120011567 ECK120011754 ECK120011771 ECK120011773 ECK120011784 ECK120011795 ECK120011798 ECK120011800 ECK120011812 ECK120011814 ECK120011862 ECK120011865 ECK120011916 ECK120011945 ECK120011947 ECK120012034 ECK120012046 ECK120012054 ECK120012058 ECK120012085 ECK120012116 ECK120012129 ECK120012137 ECK120012194 ECK120012197 ECK120012200 ECK120012257 ECK120012343 ECK120012345 ECK120012356 ECK120012359 ECK120012374 ECK120012403 ECK120012405 ECK120012438 ECK120012442 ECK120012490 ECK120012508 ECK120012523 ECK120012557 ECK120012567 ECK120012575 ECK120012583 ECK120012600 ECK120012662 ECK120012673 ECK120012702 ECK120012710 ECK120012721 ECK120012736 ECK120012738 ECK120012754 ECK120012776 ECK120012779 ECK120012830 ECK120012882 ECK120012909 ECK120012917 ECK120012949 ECK120012973 ECK120013023 ECK120013025 ECK120013030 ECK120013033 ECK120013036 ECK120013038 ECK120013041 ECK120013043 ECK120013045 ECK120013047 ECK120013051 ECK120013055 ECK120013057 ECK120013059 ECK120013287 ECK120013297 ECK120013331 ECK120013333 ECK120013340 ECK120013365 ECK120013367 ECK120013379 ECK120013388 ECK120013392 ECK120013413 ECK120013423 ECK120013437 ECK120013439 ECK120013442 ECK120013446 ECK120013466 ECK120013468 ECK120013470 ECK120013483 ECK120013489 ECK120013493 ECK120013520 ECK120013523 ECK120013545 ECK120013562 ECK120013565 ECK120013571 ECK120013574 ECK120013580 ECK120013643 ECK120013648 ECK120013651 ECK120013653 ECK120013707 ECK120013709 ECK120013711 ECK120013713 ECK120013715 ECK120013719 ECK120013721 ECK120013723 ECK120013728 ECK120013770 ECK120013797 ECK120013820 ECK120013822 ECK120013834 ECK120013889 ECK120013893 ECK120013944 ECK120013966 ECK120013972 ECK120013974 ECK120013988 ECK120013990 ECK120013996 ECK120014009 ECK120014011 ECK120014013 ECK120014032 ECK120014061 ECK120014110 ECK120014121 ECK120014126 ECK120014148 ECK120014150 ECK120014152 ECK120014163 ECK120015205 ECK120015231 ECK120015562 ECK120015669 ECK120015678 ECK120015684 ECK120015703 ECK120015745 ECK120015761 ECK120015998 ECK120016026 ECK120016028 ECK120016030 ECK120016034 ECK120016038 ECK120016040 ECK120016042 ECK120016044 ECK120016046 ECK120016048 ECK120016050 ECK120016052 ECK120016054 ECK120016149 ECK120016152 ECK120016489 ECK120016534 ECK120016824 ECK120016826 ECK120016828 ECK120016830 ECK120016832 ECK120016834 ECK120016836 ECK120016838 ECK120016840 ECK120016842 ECK120016844 ECK120016846 ECK120016848 ECK120016850 ECK120016852 ECK120016854 ECK120016856 ECK120016858 ECK120016860 ECK120016862 ECK120016864 ECK120016866 ECK120016868 ECK120016887 ECK120018496 ECK120018504 ECK120026335 ECK120026467 ECK120029481 ECK120029537 ECK120029608 ECK120030688 ECK120033077 ECK120033079 ECK120033081 ECK120034575 ECK120034894 ECK120035029 ECK120035048 ECK120048808 ECK120048830 ECK120048932 ECK120051348 ECK120051350 ECK120051352 ECK120051468 ECK125108611 ECK125108617 ECK125108619 ECK125108621 ECK125108648 ECK125110251 ECK125134898 ECK125135087 ECK125135218 ECK125135220 ECK125135222 ECK125135224 ECK125135226 ECK125135229 ECK125135236 ECK125141164 ECK125141209 ECK125141242 ECK125141244 ECK125141260 ECK125141459 ECK125141476 ECK125141477 |
Publications: | Zheng D., Constantinidou C., Hobman JL., Minchin SD. Identification of the CRP regulon using in vitro and in vivo transcriptional profiling. Nucleic Acids Res. 32(19):5874-93 (2004). [Pubmed] Nishino K., Senda Y., Yamaguchi A. CRP regulator modulates multidrug resistance of Escherichia coli by repressing the mdtEF multidrug efflux genes. J Antibiot (Tokyo). 61(3):120-7 (2008). [Pubmed] Belyaeva TA., Wade JT., Webster CL., Howard VJ., Thomas MS., Hyde EI., Busby SJ. Transcription activation at the Escherichia coli melAB promoter: the role of MelR and the cyclic AMP receptor protein. Mol Microbiol. 36(1):211-22 (2000). [Pubmed] Deutscher J. The mechanisms of carbon catabolite repression in bacteria. Curr Opin Microbiol. 11(2):87-93 (2008). [Pubmed] Gorke B., Stulke J. Carbon catabolite repression in bacteria: many ways to make the most out of nutrients. Nat Rev Microbiol. 6(8):613-24 (2008). [Pubmed] Kolb A., Busby S., Buc H., Garges S., Adhya S. Transcriptional regulation by cAMP and its receptor protein. Annu Rev Biochem. 62:749-95 (1993). [Pubmed] Landis L., Xu J., Johnson RC. The cAMP receptor protein CRP can function as an osmoregulator of transcription in Escherichia coli. Genes Dev. 13(23):3081-91 (1999). [Pubmed] Balsalobre C., Johansson J., Uhlin BE. Cyclic AMP-dependent osmoregulation of crp gene expression in Escherichia coli. J Bacteriol. 188(16):5935-44 (2006). [Pubmed] Johansson J., Balsalobre C., Wang SY., Urbonaviciene J., Jin DJ., Sonden B., Uhlin BE. Nucleoid proteins stimulate stringently controlled bacterial promoters: a link between the cAMP-CRP and the (p)ppGpp regulons in Escherichia coli. Cell. 102(4):475-85 (2000). [Pubmed] Jackson DW., Simecka JW., Romeo T. Catabolite repression of Escherichia coli biofilm formation. J Bacteriol. 184(12):3406-10 (2002). [Pubmed] Mao XJ., Huo YX., Buck M., Kolb A., Wang YP. Interplay between CRP-cAMP and PII-Ntr systems forms novel regulatory network between carbon metabolism and nitrogen assimilation in Escherichia coli. Nucleic Acids Res. 35(5):1432-40 (2007). [Pubmed] Paul L., Mishra PK., Blumenthal RM., Matthews RG. Integration of regulatory signals through involvement of multiple global regulators: control of the Escherichia coli gltBDF operon by Lrp, IHF, Crp, and ArgR. BMC Microbiol. 7:2 (2007). [Pubmed] Tian ZX., Li QS., Buck M., Kolb A., Wang YP. The CRP-cAMP complex and downregulation of the glnAp2 promoter provides a novel regulatory linkage between carbon metabolism and nitrogen assimilation in Escherichia coli. Mol Microbiol. 41(4):911-24 (2001). [Pubmed] Zhang Z., Gosset G., Barabote R., Gonzalez CS., Cuevas WA., Saier MH. Functional interactions between the carbon and iron utilization regulators, Crp and Fur, in Escherichia coli. J Bacteriol. 187(3):980-90 (2005). [Pubmed] Sinha S., Cameron AD., Redfield RJ. Sxy induces a CRP-S regulon in Escherichia coli. J Bacteriol. 191(16):5180-95 (2009). [Pubmed] Hirakawa H., Inazumi Y., Senda Y., Kobayashi A., Hirata T., Nishino K., Yamaguchi A. N-acetyl-d-glucosamine induces the expression of multidrug exporter genes, mdtEF, via catabolite activation in Escherichia coli. J Bacteriol. 188(16):5851-8 (2006). [Pubmed] De Lay N., Gottesman S. The Crp-activated small noncoding regulatory RNA CyaR (RyeE) links nutritional status to group behavior. J Bacteriol. 191(2):461-76 (2009). [Pubmed] Khankal R., Chin JW., Ghosh D., Cirino PC. Transcriptional effects of CRP* expression in Escherichia coli. J Biol Eng. 3:13 (2009). [Pubmed] Gutierrez-Rios RM., Freyre-Gonzalez JA., Resendis O., Collado-Vides J., Saier M., Gosset G. Identification of regulatory network topological units coordinating the genome-wide transcriptional response to glucose in Escherichia coli. BMC Microbiol. 7:53 (2007). [Pubmed] Gosset G., Zhang Z., Nayyar S., Cuevas WA., Saier MH. Transcriptome analysis of Crp-dependent catabolite control of gene expression in Escherichia coli. J Bacteriol. 186(11):3516-24 (2004). [Pubmed] Aiba H. Autoregulation of the Escherichia coli crp gene: CRP is a transcriptional repressor for its own gene. Cell. 32(1):141-9 (1983). [Pubmed] Hanamura A., Aiba H. A new aspect of transcriptional control of the Escherichia coli crp gene: positive autoregulation. Mol Microbiol. 6(17):2489-97 (1992). [Pubmed] Gonzalez-Gil G., Kahmann R., Muskhelishvili G. Regulation of crp transcription by oscillation between distinct nucleoprotein complexes. EMBO J. 17(10):2877-85 (1998). [Pubmed] Zubay G., Schwartz D., Beckwith J. Mechanism of activation of catabolite-sensitive genes: a positive control system. Proc Natl Acad Sci U S A. 66(1):104-10 (1970). [Pubmed] Emmer M., deCrombrugghe B., Pastan I., Perlman R. Cyclic AMP receptor protein of E. coli: its role in the synthesis of inducible enzymes. Proc Natl Acad Sci U S A. 66(2):480-7 (1970). [Pubmed] McKay DB., Steitz TA. Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA. Nature. 290(5809):744-9 (1981). [Pubmed] Aiba H., Fujimoto S., Ozaki N. Molecular cloning and nucleotide sequencing of the gene for E. coli cAMP receptor protein. Nucleic Acids Res. 10(4):1345-61 (1982). [Pubmed] Goldberg S.R, Henningfield J.E. Reinforcing effects of nicotine in humans and experimental animals responding under intermittent schedules of i.v. drug injection. Pharmacology, biochemistry, and behavior 30:227-34 (1988). [Pubmed] Blaszczyk U., Polit A., Guz A., Wasylewski Z. Interaction of cAMP receptor protein from Escherichia coli with cAMP and DNA studied by dynamic light scattering and time-resolved fluorescence anisotropy methods. J Protein Chem. 20(8):601-10 (2001). [Pubmed] Gaston K., Bell A., Kolb A., Buc H., Busby S. Stringent spacing requirements for transcription activation by CRP. Cell. 62(4):733-43 (1990). [Pubmed] Tebbutt J., Rhodius VA., Webster CL., Busby SJ. Architectural requirements for optimal activation by tandem CRP molecules at a class I CRP-dependent promoter. FEMS Microbiol Lett. 210(1):55-60 (2002). [Pubmed] Zhou Y., Pendergrast PS., Bell A., Williams R., Busby S., Ebright RH. The functional subunit of a dimeric transcription activator protein depends on promoter architecture. EMBO J. 13(19):4549-57 (1994). [Pubmed] Igarashi K., Ishihama A. Bipartite functional map of the E. coli RNA polymerase alpha subunit: involvement of the C-terminal region in transcription activation by cAMP-CRP. Cell. 65(6):1015-22 (1991). [Pubmed] Savery N., Rhodius V., Busby S. Protein-protein interactions during transcription activation: the case of the Escherichia coli cyclic AMP receptor protein. Philos Trans R Soc Lond B Biol Sci. 351(1339):543-50 (1996). [Pubmed] Ebright RH. Transcription activation at Class I CAP-dependent promoters. Mol Microbiol. 8(5):797-802 (1993). [Pubmed] Savery NJ., Lloyd GS., Kainz M., Gaal T., Ross W., Ebright RH., Gourse RL., Busby SJ. Transcription activation at Class II CRP-dependent promoters: identification of determinants in the C-terminal domain of the RNA polymerase alpha subunit. EMBO J. 17(12):3439-47 (1998). [Pubmed] Barnard A., Wolfe A., Busby S. Regulation at complex bacterial promoters: how bacteria use different promoter organizations to produce different regulatory outcomes. Curr Opin Microbiol. 7(2):102-8 (2004). [Pubmed] Beatty CM., Browning DF., Busby SJ., Wolfe AJ. Cyclic AMP receptor protein-dependent activation of the Escherichia coli acsP2 promoter by a synergistic class III mechanism. J Bacteriol. 185(17):5148-57 (2003). [Pubmed] Wade JT., Belyaeva TA., Hyde EI., Busby SJ. A simple mechanism for co-dependence on two activators at an Escherichia coli promoter. EMBO J. 20(24):7160-7 (2001). [Pubmed] Wickstrum JR., Santangelo TJ., Egan SM. Cyclic AMP receptor protein and RhaR synergistically activate transcription from the L-rhamnose-responsive rhaSR promoter in Escherichia coli. J Bacteriol. 187(19):6708-18 (2005). [Pubmed] Lobell RB., Schleif RF. AraC-DNA looping: orientation and distance-dependent loop breaking by the cyclic AMP receptor protein. J Mol Biol. 218(1):45-54 (1991). [Pubmed] Polayes DA., Rice PW., Garner MM., Dahlberg JE. Cyclic AMP-cyclic AMP receptor protein as a repressor of transcription of the spf gene of Escherichia coli. J Bacteriol. 170(7):3110-4 (1988). [Pubmed] Mollegaard NE., Rasmussen PB., Valentin-Hansen P., Nielsen PE. Characterization of promoter recognition complexes formed by CRP and CytR for repression and by CRP and RNA polymerase for activation of transcription on the Escherichia coli deoP2 promoter. J Biol Chem. 268(23):17471-7 (1993). [Pubmed] Valentin-Hansen P., Sogaard-Andersen L., Pedersen H. A flexible partnership: the CytR anti-activator and the cAMP-CRP activator protein, comrades in transcription control. Mol Microbiol. 20(3):461-6 (1996). [Pubmed] McNeill R., Sare GM., Manoharan M., Testa HJ., Mann DM., Neary D., Snowden JS., Varma AR. Accuracy of single-photon emission computed tomography in differentiating frontotemporal dementia from Alzheimer's disease. J Neurol Neurosurg Psychiatry. 78(4):350-5 (2007). [Pubmed] Perini LT., Doherty EA., Werner E., Senear DF. Multiple specific CytR binding sites at the Escherichia coli deoP2 promoter mediate both cooperative and competitive interactions between CytR and cAMP receptor protein. J Biol Chem. 271(52):33242-55 (1996). [Pubmed] Liu M., Garges S., Adhya S. lacP1 promoter with an extended -10 motif. Pleiotropic effects of cyclic AMP protein at different steps of transcription initiation. J Biol Chem. 279(52):54552-7 (2004). [Pubmed] Rostoks N., Park S., Choy HE. Reiterative transcription initiation from galP2 promoter of Escherichia coli. Biochim Biophys Acta. 1491(1-3):185-95 (2000). [Pubmed] Deutscher J., Francke C., Postma PW. How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol Mol Biol Rev. 70(4):939-1031 (2006). [Pubmed] Hogema BM., Arents JC., Bader R., Eijkemans K., Yoshida H., Takahashi H., Aiba H., Postma PW. Inducer exclusion in Escherichia coli by non-PTS substrates: the role of the PEP to pyruvate ratio in determining the phosphorylation state of enzyme IIAGlc. Mol Microbiol. 30(3):487-98 (1998). [Pubmed] Feucht BU., Saier MH. Fine control of adenylate cyclase by the phosphoenolpyruvate:sugar phosphotransferase systems in Escherichia coli and Salmonella typhimurium. J Bacteriol. 141(2):603-10 (1980). [Pubmed] Reddy P., Kamireddi M. Modulation of Escherichia coli adenylyl cyclase activity by catalytic-site mutants of protein IIA(Glc) of the phosphoenolpyruvate:sugar phosphotransferase system. J Bacteriol. 180(3):732-6 (1998). [Pubmed] Park YH., Lee BR., Seok YJ., Peterkofsky A. In vitro reconstitution of catabolite repression in Escherichia coli. J Biol Chem. 281(10):6448-54 (2006). [Pubmed] Bettenbrock K., Sauter T., Jahreis K., Kremling A., Lengeler JW., Gilles ED. Correlation between growth rates, EIIACrr phosphorylation, and intracellular cyclic AMP levels in Escherichia coli K-12. J Bacteriol. 189(19):6891-900 (2007). [Pubmed] Ishizuka H., Hanamura A., Inada T., Aiba H. Mechanism of the down-regulation of cAMP receptor protein by glucose in Escherichia coli: role of autoregulation of the crp gene. EMBO J. 13(13):3077-82 (1994). [Pubmed] Saier MH. Protein phosphorylation and allosteric control of inducer exclusion and catabolite repression by the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Microbiol Rev. 53(1):109-20 (1989). [Pubmed] Hanamura A., Aiba H. Molecular mechanism of negative autoregulation of Escherichia coli crp gene. Nucleic Acids Res. 19(16):4413-9 (1991). [Pubmed] Nelson SO., Wright JK., Postma PW. The mechanism of inducer exclusion. Direct interaction between purified III of the phosphoenolpyruvate:sugar phosphotransferase system and the lactose carrier of Escherichia coli. EMBO J. 2(5):715-720 (1983). [Pubmed] Osumi T., Saier MH. Regulation of lactose permease activity by the phosphoenolpyruvate:sugar phosphotransferase system: evidence for direct binding of the glucose-specific enzyme III to the lactose permease. Proc Natl Acad Sci U S A. 79(5):1457-61 (1982). [Pubmed] Dills SS., Schmidt MR., Saier MH. Regulation of lactose transport by the phosphoenolpyruvate-sugar phosphotransferase system in membrane vesicles of Escherichia coli. J Cell Biochem. 18(2):239-44 (1982). [Pubmed] Sondej M., Weinglass AB., Peterkofsky A., Kaback HR. Binding of enzyme IIAGlc, a component of the phosphoenolpyruvate:sugar phosphotransferase system, to the Escherichia coli lactose permease. Biochemistry. 41(17):5556-65 (2002). [Pubmed] Zhang H., Chong H., Ching CB., Jiang R. Random mutagenesis of global transcription factor cAMP receptor protein for improved osmotolerance. Biotechnol Bioeng. 109(5):1165-72 (2012). [Pubmed] Grainger DC., Hurd D., Harrison M., Holdstock J., Busby SJ. Studies of the distribution of Escherichia coli cAMP-receptor protein and RNA polymerase along the E. coli chromosome. Proc Natl Acad Sci U S A. 102(49):17693-8 (2005). [Pubmed] Robison K., McGuire AM., Church GM. A comprehensive library of DNA-binding site matrices for 55 proteins applied to the complete Escherichia coli K-12 genome. J Mol Biol. 284(2):241-54 (1998). [Pubmed] Fic E., Bonarek P., Gorecki A., Kedracka-Krok S., Mikolajczak J., Polit A., Tworzydlo M., Dziedzicka-Wasylewska M., Wasylewski Z. cAMP Receptor Protein from Escherichia coli as a Model of Signal Transduction in Proteins - A Review. J Mol Microbiol Biotechnol (2008). [Pubmed] Korner H., Sofia HJ., Zumft WG. Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. FEMS Microbiol Rev. 27(5):559-92 (2003). [Pubmed] Green J., Scott C., Guest JR. Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP. Adv Microb Physiol. 44:1-34 (2001). [Pubmed] McKay DB., Weber IT., Steitz TA. Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP. J Biol Chem. 257(16):9518-24 (1982). [Pubmed] Weber IT., Steitz TA. Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 A resolution. J Mol Biol. 198(2):311-26 (1987). [Pubmed] Passner JM., Schultz SC., Steitz TA. Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution. J Mol Biol. 304(5):847-59 (2000). [Pubmed] Schultz SC., Shields GC., Steitz TA. Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees. Science. 253(5023):1001-7 (1991). [Pubmed] Parkinson G., Wilson C., Gunasekera A., Ebright YW., Ebright RE., Berman HM. Structure of the CAP-DNA complex at 2.5 angstroms resolution: a complete picture of the protein-DNA interface. J Mol Biol. 260(3):395-408 (1996). [Pubmed] Passner JM., Steitz TA. The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer. Proc Natl Acad Sci U S A. 94(7):2843-7 (1997). [Pubmed] Benoff B., Yang H., Lawson CL., Parkinson G., Liu J., Blatter E., Ebright YW., Berman HM., Ebright RH. Structural basis of transcription activation: the CAP-alpha CTD-DNA complex. Science. 297(5586):1562-6 (2002). [Pubmed] Popovych N., Tzeng SR., Tonelli M., Ebright RH., Kalodimos CG. Structural basis for cAMP-mediated allosteric control of the catabolite activator protein. Proc Natl Acad Sci U S A. 106(17):6927-32 (2009). [Pubmed] Sharma H., Yu S., Kong J., Wang J., Steitz TA. Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proc Natl Acad Sci U S A. 106(39):16604-9 (2009). [Pubmed] Ebright RH., Ebright YW., Gunasekera A. Consensus DNA site for the Escherichia coli catabolite gene activator protein (CAP): CAP exhibits a 450-fold higher affinity for the consensus DNA site than for the E. coli lac DNA site. Nucleic Acids Res. 17(24):10295-305 (1989). [Pubmed] Wu HM., Crothers DM. The locus of sequence-directed and protein-induced DNA bending. Nature. 308(5959):509-13 (). [Pubmed] Chen S., Gunasekera A., Zhang X., Kunkel TA., Ebright RH., Berman HM. Indirect readout of DNA sequence at the primary-kink site in the CAP-DNA complex: alteration of DNA binding specificity through alteration of DNA kinking. J Mol Biol. 314(1):75-82 (2001). [Pubmed] Zhou Y., Zhang X., Ebright RH. Identification of the activating region of catabolite gene activator protein (CAP): isolation and characterization of mutants of CAP specifically defective in transcription activation. Proc Natl Acad Sci U S A. 90(13):6081-5 (1993). [Pubmed] Niu W., Zhou Y., Dong Q., Ebright YW., Ebright RH. Characterization of the activating region of Escherichia coli catabolite gene activator protein (CAP). I. Saturation and alanine-scanning mutagenesis. J Mol Biol. 243(4):595-602 (1994). [Pubmed] Niu W., Kim Y., Tau G., Heyduk T., Ebright RH. Transcription activation at class II CAP-dependent promoters: two interactions between CAP and RNA polymerase. Cell. 87(6):1123-34 (1996). [Pubmed] Busby S., Ebright RH. Transcription activation by catabolite activator protein (CAP). J Mol Biol. 293(2):199-213 (1999). [Pubmed] Ushida C., Aiba H. Helical phase dependent action of CRP: effect of the distance between the CRP site and the -35 region on promoter activity. Nucleic Acids Res. 18(21):6325-30 (1990). [Pubmed] |
Related annotations: | PaperBLAST |
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These data are available AS IS and at your own risk. The EEAD/CSIC do not give any representation or warranty nor assume any liability or responsibility for the data nor the results posted (whether as to their accuracy, completeness, quality or otherwise). Access to these data is available free of charge for ordinary use in the course of research. Downloaded data have CC-BY-NC-SA license. FootprintDB is also available at RSAT::Plants, part of the INB/ELIXIR-ES resources portfolio.