Document Detail


Characterization of FadR, a global transcriptional regulator of fatty acid metabolism in Escherichia coli. Interaction with the fadB promoter is prevented by long chain fatty acyl coenzyme A.
MedLine Citation:
PMID:  1569108     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The Escherichia coli fadR gene product, FadR, is a multifunctional regulator of fatty acid metabolism. In this work we have purified FadR by a two-step procedure employing two ion-exchange columns. The amino-terminal sequence of the purified protein confirms the sequence of the protein derived from analysis of the DNA sequence (DiRusso, C. C. (1988) Nucleic Acids Res. 16, 7995-8009) and indicates that the initiating methionine is cleaved from the mature protein. Purified FadR binds to a 326-base pair HaeIII fragment of fadB DNA which carries the fadB promoter. DNase I footprinting localizes the operator to a sequence, 5' ATCTGGTACGACCAGAT 3', at +1 to +17 nucleotides relative to the start of transcription. Using protein-DNA gel retention assays, we estimate the Keq of FadR binding to the fadB operator to be approximately 3 x 10(-10) M. Binding of FadR is specifically inhibited by long chain fatty acyl-CoA compounds. The apparent Ki values for oleoyl-CoA, palmitoyl-CoA, and palmitoleoyl-CoA are each 5 nM while that of myristoyl-CoA is 250 nM. Decanoyl-CoA, crotonoyl-CoA, and free fatty acids inhibited binding only at concentrations above 1 microM.
Authors:
C C DiRusso; T L Heimert; A K Metzger
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  267     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1992 Apr 
Date Detail:
Created Date:  1992-05-28     Completed Date:  1992-05-28     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  8685-91     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Tennessee, Memphis 38163.
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MeSH Terms
Descriptor/Qualifier:
Acyl Coenzyme A / metabolism*
Bacterial Proteins / genetics,  metabolism*
Base Sequence
Chromatography, Liquid
DNA Fingerprinting
DNA, Bacterial / genetics,  metabolism
Electrophoresis, Polyacrylamide Gel
Escherichia coli / genetics,  metabolism*
Fatty Acids / metabolism*
Molecular Sequence Data
Operator Regions, Genetic
Plasmids
Promoter Regions, Genetic*
Repressor Proteins*
Transcription, Genetic*
Grant Support
ID/Acronym/Agency:
GM38104/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Acyl Coenzyme A; 0/Bacterial Proteins; 0/DNA, Bacterial; 0/FadR protein, Bacteria; 0/Fatty Acids; 0/Repressor Proteins
Comments/Corrections
Erratum In:
J Biol Chem 1992 Nov 5;267(31):22693

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