Nucleic Acids Research, 1988, Vol. 16, No. 16 7995-8009
© 1988
Articles |
Nucleotide sequence of the fadR gene, a multifunctional regulator of fatty acid metabolism in Escherichia coli
College of Medicine, Department of Biochemistry, University of Tennessee 800 Madison Avenue, Memphis, TN 38163, USA
Received April 7, 1988. Revised July 18, 1988. Accepted July 18, 1988.
The Escherichia coli fadR gene is a multifunctional regulator of fatty acid and acetate metabolism. In the present work the nucleotide sequence of the 1.3 kb DNA fragment which encodes FadR has been determined. The coding sequence of the fadR gene is 714 nucleotides long and Is preceded by a typical E. coli ribosome binding site and is followed by a sequence predicted to be sufficient for factor-independent chain termination. Primer extension experiments demonstrated that the transcription of the fadR gene initiates with an adenine nucleotide 33 nucleotides upstream from the predicted start of translation. The derived fadR peptide has a calculated molecular weight of 26,972. This is in reasonable agreement with the apparent molecular weight of 29,000 previously estimated on the basis of maxi-cell analysis of plasmid encoded proteins. There is a segment of twenty amino acids within the predicted peptide which resembles the DNA recognition and binding site of many transcriptional regulatory proteins.
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
T. Schmelter, B. L. Trigatti, G. E. Gerber, and D. Mangroo Biochemical Demonstration of the Involvement of Fatty Acyl-CoA Synthetase in Fatty Acid Translocation across the Plasma Membrane J. Biol. Chem., June 4, 2004; 279(23): 24163 - 24170. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Rigali, A. Derouaux, F. Giannotta, and J. Dusart Subdivision of the Helix-Turn-Helix GntR Family of Bacterial Regulators in the FadR, HutC, MocR, and YtrA Subfamilies J. Biol. Chem., April 5, 2002; 277(15): 12507 - 12515. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. C. DiRusso, V. Tsvetnitsky, P. Hojrup, and J. Knudsen Fatty Acyl-CoA Binding Domain of the Transcription Factor FadR. CHARACTERIZATION BY DELETION, AFFINITY LABELING, AND ISOTHERMAL TITRATION CALORIMETRY J. Biol. Chem., December 11, 1998; 273(50): 33652 - 33659. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. K. B. Berlyn Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map Microbiol. Mol. Biol. Rev., September 1, 1998; 62(3): 814 - 984. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. N. A. Palmer, E. Axen, V. Hughes, and C. R. Wolf The Repressor Protein, Bm3R1, Mediates an Adaptive Response to Toxic Fatty Acids in Bacillus megaterium J. Biol. Chem., July 17, 1998; 273(29): 18109 - 18116. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Raman, P. N. Black, and C. C. DiRusso Characterization of the Fatty Acid-responsive Transcription Factor FadR. BIOCHEMICAL AND GENETIC ANALYSES OF THE NATIVE CONFORMATION AND FUNCTIONAL DOMAINS J. Biol. Chem., December 5, 1997; 272(49): 30645 - 30650. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Raman and C. C. DiRusso Analysis of Acyl Coenzyme A Binding to the Transcription Factor FadR and Identification of Amino Acid Residues in the Carboxyl Terminus Required for Ligand Binding J. Biol. Chem., January 20, 1995; 270(3): 1092 - 1097. [Abstract] [Full Text] [PDF] |
||||
![]() |
Y. Xu, R. J. Heath, Z. Li, C. O. Rock, and S. W. White The FadR{middle dot}DNA Complex. TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ESCHERICHIA COLI J. Biol. Chem., May 11, 2001; 276(20): 17373 - 17379. [Abstract] [Full Text] [PDF] |
||||

