Transcription Factor

Accessions: ECK120004833 (RegulonDB 7.5)
Names: GalR, GalR DNA-binding 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: The Galactose repressor, GalR, is a DNA-binding transcription factor that represses transcription of the operons involved in transport and catabolism of D-galactose Semsey S,2007; Weickert MJ,1993; Geanacopoulos M,1997; Synthesis of these operons is induced when E. coli is grown in the presence of inducer (D-galactose) and the absence glucose Geanacopoulos M,1997; Weickert MJ,1992; Weickert MJ,1993 The expression of galR is increased only in the presence of inducer Weickert MJ,1993; Geanacopoulos M,1997 In particular, in the absence of D-galactose, GalR represses the galETKM operon Aki T,1997 In this repression system, GalR binds to two operators in the presence of HU, resulting in the formation of a repressor loop Aki T,1997; Semsey S,2002; Semsey S,2004 This repressor binds in tandem to inverted repeat sequences that are 16 nucleotides long and possess conserved motifs; each dimer binds to one of these conserved sequences Weickert MJ,1993; Weickert MJ,1993 On the other hand, GalR is highly homologous in its amino acid sequence to GalS (55% identical and 88% similar); apparently both act together and are capable of cross-talk to regulate expression of the gal regulon Weickert MJ,1992; Geanacopoulos M,1997 For this reason these regulators bind the same operators, in the cis regulatory regions, with different affinities Brown MP,1994 In the presence of inductor, GalR undergoes a conformational change that reduces its affinity for the operator; Golding et al; showed that GalR is the major repressor of the gal operon Golding A,1991GalR belongs to the GalR/LacI family of transcriptional regulators; Accordingly, this transcriptional repressor family protein is composed of two domains: a conserved N-terminal domain which contains the DNA-binding region, and the carboxy-terminal domain, which is involved in effector binding and dimerization Weickert MJ,1992; Geanacopoulos M,1997 GalR and GalS have only two substitutions in the first helix of the N-terminal domain Weickert MJ,1992; carbon compounds; repressor; operon; Transcription related; cytoplasm; transcription, DNA-dependent; carbohydrate metabolic process; intracellular; sequence-specific DNA binding transcription factor activity; DNA binding; regulation of transcription, DNA-dependent
Length: 344
Pfam Domains: 3-48 Bacterial regulatory proteins, lacI family
60-296 Periplasmic binding proteins and sugar binding domain of LacI family
62-309 Periplasmic binding protein domain
169-329 Periplasmic binding protein-like domain
Sequence:
(in bold interface residues)
1 MATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQTTE 60
61 TVGLVVGDVSDPFFGAMVKAVEQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALV 120
121 VHAKMIPDADLASLMKQMPGMVLINRILPGFENRCIALDDRYGAWLATRHLIQQGHTRIG 180
181 YLCSNHSISDAEDRLQGYYDALAESGIAANDRLVTFGEPDESGGEQAMTELLGRGRNFTA 240
241 VACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAA 300
301 ELALALADNRPLPEITNVFSPTLVRRHSVSTPSLEASHHATSD*
Interface Residues: 4, 5, 14, 15, 16, 17, 19, 20, 26, 27, 28, 51, 54, 55
3D-footprint Homologues: 7ce1_D, 1efa_B, 3oqm_C, 1l1m_B, 1jft_A, 1zvv_A
Binding Motifs: GalR GwAAmYRhTwmMAyyv
Binding Sites: ECK120012718
ECK120015211
Publications: Semsey S., Krishna S., Sneppen K., Adhya S. Signal integration in the galactose network of Escherichia coli. Mol Microbiol. 65(2):465-76 (2007). [Pubmed]

Weickert MJ., Adhya S. The galactose regulon of Escherichia coli. Mol Microbiol. 10(2):245-51 (1993). [Pubmed]

Weickert MJ., Adhya S. Control of transcription of gal repressor and isorepressor genes in Escherichia coli. J Bacteriol. 175(1):251-8 (1993). [Pubmed]

Geanacopoulos M., Adhya S. Functional characterization of roles of GalR and GalS as regulators of the gal regulon. J Bacteriol. 179(1):228-34 (1997). [Pubmed]

Golding A., Weickert MJ., Tokeson JP., Garges S., Adhya S. A mutation defining ultrainduction of the Escherichia coli gal operon. J Bacteriol. 173(19):6294-6 (1991). [Pubmed]

Aki T., Adhya S. Repressor induced site-specific binding of HU for transcriptional regulation. EMBO J. 16(12):3666-74 (1997). [Pubmed]

Semsey S., Geanacopoulos M., Lewis DE., Adhya S. Operator-bound GalR dimers close DNA loops by direct interaction: tetramerization and inducer binding. EMBO J. 21(16):4349-56 (2002). [Pubmed]

Semsey S., Tolstorukov MY., Virnik K., Zhurkin VB., Adhya S. DNA trajectory in the Gal repressosome. Genes Dev. 18(15):1898-907 (2004). [Pubmed]

Brown MP., Shaikh N., Brenowitz M., Brand L. The allosteric interaction between D-galactose and the Escherichia coli galactose repressor protein. J Biol Chem. 269(17):12600-5 (1994). [Pubmed]

Weickert MJ., Adhya S. Isorepressor of the gal regulon in Escherichia coli. J Mol Biol. 226(1):69-83 (1992). [Pubmed]
Related annotations: PaperBLAST

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