title: Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli.
abstract: The primary structure of a multifunctional protein, the large alpha-subunit of the Escherichia coli fatty acid oxidation complex, was determined by sequencing the fadB region of the fadBA operon. The amino-terminal sequence of this protein had been established by Edman degradation. The transcription start site of the fadBA operon was located 42 nucleotides upstream of the initiator codon of the fadB gene by primer extension analysis. Sequences of -10 and -35 regions of the promoter responsible for interaction with RNA polymerase were found to be CACACT and TTTGCA, respectively. The location of the promoter of the fadBA operon was defined, and the transcription direction of this operon, from fadB to fadA, as previously proposed [Yang, S.-Y., et al. (1990) J. Biol. Chem. 265, 10424-10429], was corroborated. The multifunctional protein is composed of 729 amino acid residues and has a calculated Mr of 79,593. A putative NAD-binding beta alpha beta-fold necessary for L-3-hydroxyacyl-CoA dehydrogenase function was found in the central region of the fadB gene product. Sequence analyses suggest that the functional domains of the multifunctional protein are arranged in the order enoyl-CoA hydratase:L-3-hydroxyacyl-CoA dehydrogenase: delta 3-cis-delta 2-trans-enoyl-CoA isomerase and suggest that the genes of the E. coli multifunctional protein and rat peroxisomal trifunctional beta-oxidation enzyme evolved from a common ancestral gene.
authors.affiliation: Laboratory of Neurobiochemistry, New York State Institute for Basic Research in Developmental Disabilities, Staten Island 10314.
authors.forename: X Y
authors.initials: XY
authors.lastname: Yang
authors.forename: H
authors.initials: H
authors.lastname: Schulz
authors.forename: M
authors.initials: M
authors.lastname: Elzinga
authors.forename: S Y
authors.initials: SY
authors.lastname: Yang
mesh_terms: D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000235:genetics* / Q000378:metabolism; D000102:Acetyl-CoA C-Acyltransferase / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D019748:Carbon-Carbon Double Bond Isomerases; D004269:DNA, Bacterial; D004746:Enoyl-CoA Hydratase / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D007535:Isomerases / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D009876:Operon; D010957:Plasmids; D011401:Promoter Regions, Genetic; D012329:RNA, Bacterial / Q000235:genetics; D019998:Racemases and Epimerases / Q000235:genetics* / Q000378:metabolism; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D013552:Swine; D014158:Transcription, Genetic
chemical_list: D004269:DNA, Bacterial; D012329:RNA, Bacterial; C038784:fatty acid oxidation complex; D015094:3-Hydroxyacyl CoA Dehydrogenases; D000102:Acetyl-CoA C-Acyltransferase; D004746:Enoyl-CoA Hydratase; D007535:Isomerases; D019998:Racemases and Epimerases; D019748:Carbon-Carbon Double Bond Isomerases