Transcription Factor
| Accessions: | ECK120005016 (RegulonDB 7.5) |
| Names: | Lrp, Lrp 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: | Lrp, Leucine-responsive regulatory protein, is a dual transcriptional regulator for at least 10% of the genes in Escherichia coli Tani TH,2002 These genes are involved in amino acid biosynthesis and catabolism, nutrient transport, pili synthesis, and other cellular functions, including 1-carbon metabolism Ernsting BR,1992; Brinkman AB,2003; Calvo JM,1994 In addition, Lrp affects nearly three-fourths of the genes induced upon entry into stationary phase Tani TH,2002; Cho BK,2008 Lrp might also play a topological role in dynamic DNA packaging D'Ari R,1993Lrp can act as a repressor or activator for its target genes; Binding of leucine can affect these activities in three different ways: leucine either potentiates, antagonizes, or has no discernible effect upon Lrp action Lin R,1992; Platko JV,1993; Newman EB,1995 It is believed that Lrp senses the presence of rich nutrition based on the concentration of leucine and positively regulates genes that function during famine and negatively regulates genes that function during a feast Calvo JM,1994Lrp forms a mixture of octamers and hexadecamers Chen S,2001 In the presence of leucine, the octamer configuration is favored; It is believed that the switch between the octameric and hexadecameric states modulated by leucine affects the binding and the activity of Lrp at its target genes Chen S,2002 The structure of Lrp from Escherichia coli bound to DNA as an octamer has been solved de los Rios S,2007 Lrp forms an open ring structure, in which the DNA is wrapped around the octamer in a nucleosome-like structure; The monomer chain contains two domains, an N-terminal helix-turn-helix motif and a C-terminal αβ-sandwich fold; The N-terminal is responsible for the specificity and function among members of the Lrp regulon across the Enterobacteriaceae; The N-terminal tail plays a significant role in modulating Lrp function, similar to what has been reported for a number of other transcriptional regulators Hart BR,2011N-terminal diversity is responsible for some of the differences between orthologs in terms of DNA binding and multimerization Hart BR,2011Lrp-regulated promoters commonly contain multiple adjacent binding sites for the protein with low sequence specificity; A consensus recognition sequence has been described Cui Y,1996 The identified 15-bp sequence motif is structured with flanking CAG/CTG triplets and a central AT-rich signal; Leucine has two effects upon binding to DNA in vitro: the affinity of Lrp is reduced but the cooperativity of binding to multiple sites is increased Chen S,2005Lrp belongs to the Lrp/AsnC family of transcriptional regulatory proteins, which is widely distributed throughout the eubacterial and archaeal domains; Lrp appears to be very well conserved in members of the γ-proteobacteria Brinkman AB,2003A microarray analysis for Lrp of Escherichia coli was done by Hung SP,2002.; regulation of transcription, DNA-dependent; sequence-specific DNA binding; response to leucine; cytoplasm; nucleoproteins, basic proteins; Transcription related; intracellular; operon; repressor; isoleucine/valine; leucine; leucine biosynthetic process; sequence-specific DNA binding transcription factor activity; activator |
| Length: | 165 |
| Pfam Domains: | 12-53 AsnC-type helix-turn-helix domain 12-59 Winged helix-turn-helix DNA-binding 78-152 AsnC family |
| Sequence: (in bold interface residues) | 1 MVDSKKRPGKDLDRIDRNILNELQKDGRISNVELSKRVGLSPTPCLERVRRLERQGFIQG 60 61 YTALLNPHYLDASLLVFVEITLNRGAPDVFEQFNTAVQKLEEIQECHLVSGDFDYLLKTR 120 121 VPDMSAYRKLLGETLLRLPGVNDTRTYVVMEEVKQSNRLVIKTR* |
| Interface Residues: | 31, 32, 41, 42, 43, 44, 46, 65 |
| 3D-footprint Homologues: | 2e1c_A, 8c7u_A |
| Binding Motifs: | Lrp awttTtwTkCtk |
| Binding Sites: | ECK120011386 ECK120011632 ECK120011637 ECK120011642 ECK120011648 ECK120011808 ECK120011810 ECK120012411 ECK120012931 ECK120012933 ECK120012935 ECK120012937 ECK120012939 ECK120012941 ECK120012947 ECK120013168 ECK120013170 ECK120013172 ECK120013269 ECK120013271 ECK120013273 ECK120013277 ECK120013349 ECK120013351 ECK120013353 ECK120013400 ECK120013501 ECK120013659 ECK120013763 ECK120013765 ECK120013767 ECK120013839 ECK120013843 ECK120013849 ECK120013853 ECK120013871 ECK120013884 ECK120013886 ECK120013914 ECK120013918 ECK120013922 ECK120013926 ECK120013930 ECK120013976 ECK120013978 ECK120013980 ECK120016176 ECK120016192 ECK120016195 ECK120034483 ECK120034485 ECK120034487 ECK120034489 ECK120034491 ECK120034493 ECK120035006 ECK120035008 ECK120035010 ECK120035018 ECK120035020 ECK120035022 ECK120048918 ECK120048920 ECK120048922 ECK120048924 ECK120048926 ECK120048928 ECK125108671 ECK125108673 ECK125108675 ECK125141480 ECK125141481 ECK125141482 ECK125141483 ECK125141484 ECK125141485 |
| Publications: | Tani TH., Khodursky A., Blumenthal RM., Brown PO., Matthews RG. Adaptation to famine: a family of stationary-phase genes revealed by microarray analysis. Proc Natl Acad Sci U S A. 99(21):13471-6 (2002). [Pubmed] Ernsting BR., Atkinson MR., Ninfa AJ., Matthews RG. Characterization of the regulon controlled by the leucine-responsive regulatory protein in Escherichia coli. J Bacteriol. 174(4):1109-18 (1992). [Pubmed] Brinkman AB., Ettema TJ., de Vos WM., van der Oost J. The Lrp family of transcriptional regulators. Mol Microbiol. 48(2):287-94 (2003). [Pubmed] Calvo JM., Matthews RG. The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli. Microbiol Rev. 58(3):466-90 (1994). [Pubmed] Cho BK., Barrett CL., Knight EM., Park YS., Palsson BO. Genome-scale reconstruction of the Lrp regulatory network in Escherichia coli. Proc Natl Acad Sci U S A. 105(49):19462-7 (2008). [Pubmed] D'Ari R., Lin RT., Newman EB. The leucine-responsive regulatory protein: more than a regulator? Trends Biochem Sci. 18(7):260-3 (1993). [Pubmed] Lin R., D'Ari R., Newman EB. Lambda placMu insertions in genes of the leucine regulon: extension of the regulon to genes not regulated by leucine. J Bacteriol. 174(6):1948-55 (1992). [Pubmed] Platko JV., Calvo JM. Mutations affecting the ability of Escherichia coli Lrp to bind DNA, activate transcription, or respond to leucine. J Bacteriol. 175(4):1110-7 (1993). [Pubmed] Newman EB., Lin R. Leucine-responsive regulatory protein: a global regulator of gene expression in E. coli. Annu Rev Microbiol. 49:747-75 (1995). [Pubmed] Chen S., Rosner MH., Calvo JM. Leucine-regulated self-association of leucine-responsive regulatory protein (Lrp) from Escherichia coli. J Mol Biol. 312(4):625-35 (2001). [Pubmed] Chen S., Calvo JM. Leucine-induced dissociation of Escherichia coli Lrp hexadecamers to octamers. J Mol Biol. 318(4):1031-42 (2002). [Pubmed] de los Rios S., Perona JJ. Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly. J Mol Biol. 366(5):1589-602 (2007). [Pubmed] Hart BR., Mishra PK., Lintner RE., Hinerman JM., Herr AB., Blumenthal RM. Recognition of DNA by the helix-turn-helix global regulatory protein lrp is modulated by the amino terminus. J Bacteriol. 193(15):3794-803 (2011). [Pubmed] Cui Y., Midkiff MA., Wang Q., Calvo JM. The leucine-responsive regulatory protein (Lrp) from Escherichia coli. Stoichiometry and minimal requirements for binding to DNA. J Biol Chem. 271(12):6611-7 (1996). [Pubmed] Chen S., Iannolo M., Calvo JM. Cooperative binding of the leucine-responsive regulatory protein (Lrp) to DNA. J Mol Biol. 345(2):251-64 (2005). [Pubmed] Hung SP., Baldi P., Hatfield GW. Global gene expression profiling in Escherichia coli K12. The effects of leucine-responsive regulatory protein. J Biol Chem. 277(43):40309-23 (2002). [Pubmed] |
| Related annotations: | PaperBLAST |
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