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Gene Review

tyrR  -  aromatic amino acid biosynthesis and...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1319, JW1316
 
 
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Disease relevance of tyrR

  • Codon usage in the tyrR structural gene shows a bias toward those synonymic codons which are used rarely in efficiently expressed E. coli genes [1].
  • Cloning and random mutagenesis of the Erwinia herbicola tyrR gene for high-level expression of tyrosine phenol-lyase [2].
 

High impact information on tyrR

 

Chemical compound and disease context of tyrR

  • A gene locus (linR) responsible for the lincomycin resistance phenotype was mapped at min 30 of the Escherichia coli chromosome near tyrR; it seems to be identical to the previously described linB locus (Apirion, 1967); however, in contrast to these reports it does not seem to alter any ribosomal function [5].
 

Biological context of tyrR

  • The nucleotide sequence of a 22-base pair region adjacent to the promoter and distal to the structural gene exhibits considerable identity with corresponding regions of other genes regulated by tyrR [1].
  • These properties were attributed to a mutation in a regulator gene, tyrR (linked to pyr F), that resulted in altered or non-functional aporepressor [6].
  • Hence tyrO, tyrA, and aroF constitute an operon regulated by tyrR [6].
  • DNA fragments containing the regulatory regions of two genes repressed by the tyrR gene product exhibit retarded electrophoretic mobility in polyacrylamide gels indicating the presence of static bends in the DNA [7].
 

Associations of tyrR with chemical compounds

  • In activation-defective tyrR mutants, expression of mtr is repressed in the presence of tyrosine [8].
  • Chromatography of cell extracts on diethylaminoethyl-Sephadex allowed partial separation of two shikimate kinase enzymes and demonstrated that only one of these subject to specific repression control involving tyrR [9].
 

Other interactions of tyrR

  • A comparison between the tyrB operator and those of the other genes belonging to the tyrR regulon is presented [10].
  • When the genes were linked in tandem and co-expressed in a plasmid, the relative AroP transport activity of the strain harboring aroP(p) -tyrR (0.95) was significantly lower than that of aroP-tyrR (1.31) [11].

References

  1. Structure of the Escherichia coli K12 regulatory gene tyrR. Nucleotide sequence and sites of initiation of transcription and translation. Cornish, E.C., Argyropoulos, V.P., Pittard, J., Davidson, B.E. J. Biol. Chem. (1986) [Pubmed]
  2. Cloning and random mutagenesis of the Erwinia herbicola tyrR gene for high-level expression of tyrosine phenol-lyase. Katayama, T., Suzuki, H., Koyanagi, T., Kumagai, H. Appl. Environ. Microbiol. (2000) [Pubmed]
  3. Isolated operator binding and ligand response domains of the TyrR protein of Haemophilus influenzae associate to reconstitute functional repressor. Zhao, S., Somerville, R.L. J. Biol. Chem. (1999) [Pubmed]
  4. Operator mutations of the Escherichia coli aroF gene. Garner, C.C., Herrmann, K.M. J. Biol. Chem. (1985) [Pubmed]
  5. Analysis of lincomycin resistance mutations in Escherichia coli. Hummel, H., Piepersberg, W., Böck, A. Mol. Gen. Genet. (1979) [Pubmed]
  6. Regulation of tyrosine and phenylalanine biosynthesis in Salmonella. Sprinson, D.B., Gollub, E.G., Hu, R.C., Liu, K.P. Acta microbiologica Academiae Scientiarum Hungaricae. (1976) [Pubmed]
  7. The role of a static bend in the DNA of the aroF regulatory region of Escherichia coli. Cobbett, C., Dickson, B., Farmer, L. Gene (1989) [Pubmed]
  8. Mutations in the tyrR gene of Escherichia coli which affect TyrR-mediated activation but not TyrR-mediated repression. Yang, J., Camakaris, H., Pittard, A.J. J. Bacteriol. (1993) [Pubmed]
  9. Aromatic amino acid biosynthesis: regulation of shikimate kinase in Escherichia coli K-12. Ely, B., Pittard, J. J. Bacteriol. (1979) [Pubmed]
  10. Molecular analysis of the regulatory region of the Escherichia coli K-12 tyrB gene. Yang, J., Pittard, J. J. Bacteriol. (1987) [Pubmed]
  11. Regulation of aroP expression by tyrR gene in Escherichia coli. Wang, J.G., Fan, C.S., Wu, Y.Q., Jin, R.L., Liu, D.X., Shang, L., Jiang, P.H. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (2003) [Pubmed]
 
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