Transcription Factor

Accessions: ECK120005057 (RegulonDB 7.5)
Names: MetJ, MetJ transcriptional repressor
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: methionine; cytoplasm; transcription, DNA-dependent; methionine biosynthetic process; DNA binding; sequence-specific DNA binding transcription factor activity; repressor; cellular amino acid biosynthetic process; regulation of transcription, DNA-dependent; Transcription related; operon; methionine metabolic process
Length: 106
Pfam Domains: 2-105 Met Apo-repressor, MetJ
Sequence:
(in bold interface residues)
1 MAEWSGEYISPYAEHGKKSEQVKKITVSIPLKVLKILTDERTRRQVNNLRHATNSELLCE 60
61 AFLHAFTGQPLPDDADLRKERSDEIPEAAKEIMREMGINPETWEY*
Interface Residues: 3, 4, 8, 9, 24, 26, 43, 67
3D-footprint Homologues: 6crm_A, 1mjo_B, 6mrj_D, 1zgw_A
Binding Motifs: MetJ rGAtGTm
Binding Sites: ECK120011475
ECK120011477
ECK120011828
ECK120011830
ECK120011832
ECK120011834
ECK120011836
ECK120011838
ECK120011840
ECK120011842
ECK120011844
ECK120011846
ECK120011848
ECK120011850
ECK120011852
ECK120011854
ECK120012792
ECK120012794
ECK120012796
ECK120012798
ECK120012800
ECK120015717
ECK120015721
ECK120048841
ECK120048843
ECK120048845
ECK120048847
Publications: Phillips K., Phillips SE. Electrostatic activation of Escherichia coli methionine repressor. Structure. 2(4):309-16 (1994). [Pubmed]

Parsons ID., Persson B., Mekhalfia A., Blackburn GM., Stockley PG. Probing the molecular mechanism of action of co-repressor in the E. coli methionine repressor-operator complex using surface plasmon resonance (SPR). Nucleic Acids Res. 23(2):211-6 (1995). [Pubmed]

Old IG., Phillips SE., Stockley PG., Saint Girons I. Regulation of methionine biosynthesis in the Enterobacteriaceae. Prog Biophys Mol Biol. 56(3):145-85 (1991). [Pubmed]

Marincs F., Manfield IW., Stead JA., McDowall KJ., Stockley PG. Transcript analysis reveals an extended regulon and the importance of protein-protein co-operativity for the Escherichia coli methionine repressor. Biochem J. 396(2):227-34 (2006). [Pubmed]

Weissbach H., Brot N. Regulation of methionine synthesis in Escherichia coli. Mol Microbiol. 5(7):1593-7 (1991). [Pubmed]

Somers WS., Phillips SE. Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands. Nature. 359(6394):387-93 (1992). [Pubmed]

Smith AA., Greene RC., Kirby TW., Hindenach BR. Isolation and characterization of the product of the methionine-regulatory gene metJ of Escherichia coli K-12. Proc Natl Acad Sci U S A. 82(18):6104-8 (1985). [Pubmed]

Saint-Girons I., Duchange N., Cohen GN., Zakin MM. Structure and autoregulation of the metJ regulatory gene in Escherichia coli. J Biol Chem. 259(22):14282-5 (1984). [Pubmed]

Phillips SE., Manfield I., Parsons I., Davidson BE., Rafferty JB., Somers WS., Margarita D., Cohen GN., Saint-Girons I., Stockley PG. Cooperative tandem binding of met repressor of Escherichia coli. Nature. 341(6244):711-5 (1989). [Pubmed]

Belfaiza J., Parsot C., Martel A., de la Tour CB., Margarita D., Cohen GN., Saint-Girons I. Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region. Proc Natl Acad Sci U S A. 83(4):867-71 (1986). [Pubmed]

Augustus AM., Reardon PN., Spicer LD. MetJ repressor interactions with DNA probed by in-cell NMR. Proc Natl Acad Sci U S A. 106(13):5065-9 (2009). [Pubmed]

Hyre DE., Spicer LD. Thermodynamic evaluation of binding interactions in the methionine repressor system of Escherichia coli using isothermal titration calorimetry. Biochemistry. 34(10):3212-21 (1995). [Pubmed]

LaMonte BL., Hughes JA. In vivo hydrolysis of S-adenosylmethionine induces the met regulon of Escherichia coli. Microbiology. 152(Pt 5):1451-9 (2006). [Pubmed]
Related annotations: PaperBLAST

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