Regulated expression of a repressor protein: FadR activates iclR

Journal of Bacteriology

Volumn 178, Issue 15, 1996, Pages 4704-4709

  Gui, Lizhen ^a   Sunnarborg, Alden ^a   Laporte, David C ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

REPRESSOR PROTEIN;

ARTICLE; CONTROLLED STUDY; DNA BINDING; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENE REPRESSION; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; REPRESSOR GENE;

ESCHERICHIA COLI;

EID: 9344239860     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.15.4704-4709.1996     Document Type: Article

References (33)

1. Borthwick, A. C., W. H. Holms, and H. G. Nimmo. 1984. The phosphorylation of Escherichia coli isocitrate dehydrogenase in intact cells. Biochem. J. 222:797-804.
2. Chung, T., D. J. Klumpp, and D. C. LaPorte. 1988. Glyoxylate bypass operon of Escherichia coli: cloning and determination of the functional map. J. Bacteriol. 170:386-392.
3. Chung, T., E. Resnik, C. Stueland, and D. C. LaPorte. 1993. Relative expression of the products of glyoxylate bypass operon: contributions of transcription and translation. J. Bacteriol. 175:4572-4575.
4. Collado-Vides, J., B. Magasanik, and J. D. Gralla. 1991. Control site location and transcriptional regulation in Escherichia coli. Microbiol. Rev. 55:371-394.
5. DiRusso, C., T. L. Heimert, and A. K. Metzger. 1992. Characterization of FadR, a global transcriptional regulator of fatty acid metabolism: interaction with the fadB promoter is prevented by long chain fatty acyl coenzyme As. J. Biol. Chem. 267:8685-8691.
6. DiRusso, C. C. 1988. Nucleotide sequence of the fadR gene, a multifunctional regulator of fatty acid metabolism in Escherichia coli. Nucleic Acids Res. 16:7995-8009.
7. Garnak, M., and H. C. Reeves. 1979. Phosphorylation of isocitrate dehydrogenase of Escherichia coli. Science 203:1111-1112.
8. Gui, L., A. R. Sunnarborg, B. Pan, and D. C. LaPorte. 1996. Autoregulation of iclR, the repressor of the glyoxylate bypass operon. J. Bacteriol. 178:321-324.
9. Henry, M. F., and J. E. J. Cronan. 1991. Escherichia coli transcription factor that both activates fatty acid synthesis and represses fatty acid degradation. J. Biol. Chem. 222:843-849.
10. Henry, M. F., and J. E. J. Cronan. 1992. A new mechanism of transcriptional regulation: release of an activator triggered by small molecule binding. Cell 70:671-679.
11. Kohara, Y., K. Akiyama, and K. Isono. 1987. The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50:495-508.
12. Kornberg, H. L. 1966. The role and control of the glyoxylate cycle in Escherichia coli. Biochem. J. 99:1-11.
13. Kornberg, H. L. 1967. The regulation of anaplerotic enzymes in E. coli. Bull. Biochem. Soc. Chim. Biol. 49:1479-1490.
14. Kornberg, H. L., and N. B. Madsen. 1951. Synthesis of C4-dicarboxylic acids from acetate by a "glyoxylate bypass" of the tricarboxylic acid cycle. Biochim. Biophys. Acta 24:651-653.
15. LaPorte, D. C., and D. E. Koshland, Jr. 1982. A protein with kinase and phosphatase activities involved in the regulation of the tricarboxylic acid cycle. Nature (London) 300:458-460.
16. LaPorte, D. C., C. S. Stueland, and T. Ikeda. 1989. Isocitrate dehydrogenase kinase/phosphatase. Biochimie 71:1051-1057.
17. LaPorte, D. C., P. E. Thorsness, and D. E. Koshland, Jr. 1985. Compensatory phosphorylation of isocitrate dehydrogenase: a mechanism for adaptation to the intracellular environment. J. Biol. Chem. 260:10563-10568.
18. LaPorte, D. C., K. Walsh, and D. E. Koshland, Jr. 1984. The branch point effect: ultrasensitivity and subsensitivity to metabolic control. J. Biol. Chem. 259:14068-14075.
19. Maloy, S. R., M. Bohlander, and W. D. Nunn. 1980. Elevated levels of glyoxylate shunt enzymes in Escherichia coli strains constitutive for tatty acid degradation. J. Bacteriol. 143:720-725.
20. Maloy, S. R., and W. D. Nunn. 1982. Genetic regulation of the glyoxylate shunt in Escherichia coli K-12. J. Bacteriol. 149:173-180.
21. Maxam, A. M., and W. Gilbert. 1980. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 65:499-560.
22. Mead, D. A., E. Szczesna-Skorupa, and B. Kemper. 1986. Single-strand DNA 'blue' T7 promoter plasmids: a versatile tandem promoter system for cloning and protein engineering. Protein Eng. 1:67-74.
23. Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
24. Negre, D., J.-C. Cortay, A. Galinier, P. Sauve, and A. J. Cozzone. 1992. Specific interactions between the IclR repressor of the acetate operon of Escherichia coli and its operator. J. Mol. Biol. 228:23-29.
25. Neidhardt, F. C., P. L. Bloch, and D. F. Smith. 1974. Culture medium for enterobacteria. J. Bacteriol. 119:735-747.
26. Nunn, W. D. 1986. A molecular view of fatty acid catabolism in Escherichia coli. Microbiol. Rev. 50:179-192.
27. Pan, B., I. Unnikrishnan, and D. C. LaPorte. 1996. The binding site of the IclR repressor protein overlaps the promoter of aceBAK. J. Bacteriol. 178:3982-3984.
28. Pollock, R., and R. Treisman. 1990. A sensitive method for the determination of protein-DNA binding specificities. Nucleic Acids Res. 18:6197-6204.
29. Resnik, E., and D. C. LaPorte. 1991. Introduction of single copy sequences into the chromosome of Escherichia coli: application to gene and operon fusions. Gene 107:19-25.
30. Resnik, E., B. Pan, N. Ramani, M. Freundlich, and D. C. LaPorte. 1996. Integration host factor amplifies the induction of the aceBAK operon by relieving IclR repression. J. Bacteriol. 178:2715-2717.
31. Sanger, F., and A. R. Coulson. 1975. A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase. J. Mol. Biol. 94:441-448.
32. Shih, H.-M., and H. C. Towle. 1992. Definition of the carbohydrate response clement of the rat S14 gene. J. Biol. Chem. 267:13222-13228.
33. Sunnarborg, A., D. Klumpp, T. Chung, and D. C. LaPorte. 1990. Regulation of the glyoxylate bypass operon: cloning and characterization of iclR. J. Bacteriol. 172:2642-2649.