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Gene Review

pIGAL1_02  -  repressor

Escherichia coli

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Disease relevance of pIGAL1_02

  • Positive and negative regulation of the Mu operator by Mu repressor and Escherichia coli integration host factor [1].
  • (iv) Only a small fraction of the lysogens in a culture spontaneously induce and when the lysogen carries two lambdoid prophages with different repressor/operators, 933W and H-19B, usually both prophages in the same cell are induced [2].
  • Separate E. coli K-12 RV308 host strains containing the new recombinants were lysogenized with the repressor-defective bacteriophage lambda cI90 [3].
  • We have examined the positions of contact between lambda phage repressor protein and operator OR1 DNA by scanning populations of lightly depurinated or depyrimidated DNA for bases essential to or irrelevant to repressor binding [4].
  • The Bacillus subtilis phage phi 105 repressor, a lambda repressor-like transcriptional regulatory protein, was overproduced in Escherichia coli and purified to near homogeneity in order to examine its in vitro DNA-binding properties [5].

High impact information on pIGAL1_02

  • Regulation of transcription initiation is generally attributable to activator/repressor proteins that bind to specific DNA sequences [6].
  • Purified Mu repressor, in addition to its primary binding in the operator region, also binds less strongly to the Mu ends at the same sites as the Mu A protein [7].
  • E. coli ribosomal protein L1 is a translational repressor of the synthesis in vitro of both proteins encoded in the L11 operon (L11 and L1) [8].
  • Feedback regulation of ribosomal protein synthesis in E. coli: localization of the mRNA target sites for repressor action of ribosomal protein L1 [8].
  • Although previous work indicated that translationally inhibited ribosomal protein mRNA is degraded in vivo, L1 repressor action in the present in vitro system was found not to involve mRNA degradation [8].

Chemical compound and disease context of pIGAL1_02


Biological context of pIGAL1_02


Anatomical context of pIGAL1_02


Associations of pIGAL1_02 with chemical compounds


Regulatory relationships of pIGAL1_02

  • The results demonstrate that expression of the resistance gene tetA is regulated by Tet repressor bound to either O1 or O2 [21].

Other interactions of pIGAL1_02

  • A two-plasmid system in which one plasmid served as substrate while the other encoded both resolvase and a thermolabile repressor of resolvase transcription provided controlled, synchronous recombination [22].
  • Expression of the repressor gene tetR is only marginally reduced when Tet repressor is bound to O2 [21].
  • Mutations in three of the four cysteine residues of merR resulted in complete loss of Hg(II)-inducible activation but retention of the repressor function, suggesting that these residues serve as ligands for Hg(II) in the activation process [23].
  • We propose that two similar regions of dyad symmetry within the Tn10 tet regulatory region are operator sites at which tet repressor binds to tet DNA, thereby inhibiting transcription initiation at the tetA and tetR promoters [24].
  • We have localized the D108 thermosensitive (cts) repressor gene to a region of DNA approx. 600 base pairs (bp) in length by sub-cloning an RsaI restriction endonuclease fragment (bp 200 to bp 802 from the left-end of the D108 genome) [25].

Analytical, diagnostic and therapeutic context of pIGAL1_02


  1. Positive and negative regulation of the Mu operator by Mu repressor and Escherichia coli integration host factor. Krause, H.M., Higgins, N.P. J. Biol. Chem. (1986) [Pubmed]
  2. Characterizing spontaneous induction of Stx encoding phages using a selectable reporter system. Livny, J., Friedman, D.I. Mol. Microbiol. (2004) [Pubmed]
  3. Selective retention of recombinant plasmids coding for human insulin. Rosteck, P.R., Hershberger, C.L. Gene (1983) [Pubmed]
  4. Missing contact probing of DNA-protein interactions. Brunelle, A., Schleif, R.F. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  5. Purification and in vitro DNA-binding specificity of the Bacillus subtilis phage phi 105 repressor. Van Kaer, L., Van Montagu, M., Dhaese, P. J. Biol. Chem. (1989) [Pubmed]
  6. rRNA promoter regulation by nonoptimal binding of sigma region 1.2: an additional recognition element for RNA polymerase. Haugen, S.P., Berkmen, M.B., Ross, W., Gaal, T., Ward, C., Gourse, R.L. Cell (2006) [Pubmed]
  7. Site-specific recognition of the bacteriophage Mu ends by the Mu A protein. Craigie, R., Mizuuchi, M., Mizuuchi, K. Cell (1984) [Pubmed]
  8. Feedback regulation of ribosomal protein synthesis in E. coli: localization of the mRNA target sites for repressor action of ribosomal protein L1. Yates, J.L., Nomura, M. Cell (1981) [Pubmed]
  9. Chemical conversion of a DNA-binding protein into a site-specific nuclease. Chen, C.H., Sigman, D.S. Science (1987) [Pubmed]
  10. NH2-terminal arm of phage lambda repressor contributes energy and specificity to repressor binding and determines the effects of operator mutations. Eliason, J.L., Weiss, M.A., Ptashne, M. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  11. Overproduction and rapid purification of the biotin operon repressor from Escherichia coli. Buoncristiani, M.R., Otsuka, A.J. J. Biol. Chem. (1988) [Pubmed]
  12. Evidence for cooperativity between the four binding sites of dimeric ArsD, an As(III)-responsive transcriptional regulator. Li, S., Rosen, B.P., Borges-Walmsley, M.I., Walmsley, A.R. J. Biol. Chem. (2002) [Pubmed]
  13. Constitutive expression of tetracycline resistance mediated by a Tn10-like element in Haemophilus parainfluenzae results from a mutation in the repressor gene. Heuer, C., Hickman, R.K., Curiale, M.S., Hillen, W., Levy, S.B. J. Bacteriol. (1987) [Pubmed]
  14. Escherichia coli RNA polymerase binding sites and transcription initiation sites in the transposon Tn3. Wishart, W.L., Machida, C., Ohtsubo, H., Ohtsubo, E. Gene (1983) [Pubmed]
  15. The chromosomal arsR gene of Escherichia coli encodes a trans-acting metalloregulatory protein. Xu, C., Shi, W., Rosen, B.P. J. Biol. Chem. (1996) [Pubmed]
  16. Purification and DNA binding properties of the blaI gene product, repressor for the beta-lactamase gene, blaP, of Bacillus licheniformis. Grossman, M.J., Lampen, J.O. Nucleic Acids Res. (1987) [Pubmed]
  17. On the transcriptional regulation of methicillin resistance: MecI repressor in complex with its operator. García-Castellanos, R., Mallorquí-Fernández, G., Marrero, A., Potempa, J., Coll, M., Gomis-Rüth, F.X. J. Biol. Chem. (2004) [Pubmed]
  18. Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator. Weaver, L.H., Kwon, K., Beckett, D., Matthews, B.W. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  19. Cyclic AMP-dependent constitutive expression of gal operon: use of repressor titration to isolate operator mutations. Irani, M., Orosz, L., Busby, S., Taniguchi, T., Adhya, S. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  20. Engineered Tet repressor mutants with single tryptophan residues as fluorescent probes. Solvent accessibilities of DNA and inducer binding sites and interaction with tetracycline. Hansen, D., Altschmied, L., Hillen, W. J. Biol. Chem. (1987) [Pubmed]
  21. Differential regulation of the Tn10-encoded tetracycline resistance genes tetA and tetR by the tandem tet operators O1 and O2. Meier, I., Wray, L.V., Hillen, W. EMBO J. (1988) [Pubmed]
  22. Mechanism of Tn3 resolvase recombination in vivo. Bliska, J.B., Benjamin, H.W., Cozzarelli, N.R. J. Biol. Chem. (1991) [Pubmed]
  23. Genetic analysis of transcriptional activation and repression in the Tn21 mer operon. Ross, W., Park, S.J., Summers, A.O. J. Bacteriol. (1989) [Pubmed]
  24. Overlapping divergent promoters control expression of Tn10 tetracycline resistance. Bertrand, K.P., Postle, K., Wray, L.V., Reznikoff, W.S. Gene (1983) [Pubmed]
  25. Cloning and localization of the repressor gene (c) of the Mu-like transposable phage D108. Levin, D.B., DuBow, M.S. FEBS Lett. (1987) [Pubmed]
  26. Crystallization of the bifunctional biotin operon repressor. Brennan, R.G., Vasu, S., Matthews, B.W., Otsuka, A.J. J. Biol. Chem. (1989) [Pubmed]
  27. DNA conformational change in Gal repressor-operator complex: involvement of central G-C base pair(s) of dyad symmetry. Wartell, R.M., Adhya, S. Nucleic Acids Res. (1988) [Pubmed]
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