This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Sugino, H Articles by Murooka, Y Search for Related Content PubMed PubMed Citation Articles by Sugino, H Articles by Murooka, Y

research-article

A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene.

Department of Fermentation Technology, Faculty of Engineering, Hiroshima University, Japan.

ABSTRACT

The Klebsiella aerogenes gene maoA, which is involved in the synthesis of monoamine oxidase, was induced by tyramine and the related compounds, subjected to catabolite and ammonium ion repression, and cloned. The nucleotide sequence of the region involved in monoamine oxidase synthesis was determined. Two open reading frames, the maoA gene and a hitherto unknown gene (maoC), were found. These are located between a potential promoter sequence and a transcriptional terminator sequence. A region of the Escherichia coli chromosome that was highly homologous to the Klebsiella maoA gene was found. The potential maoA gene is located at 30.9 min on the E. coli chromosome. Analysis of the amino acid sequences of the first 11 amino acids from the N terminus of the purified monoamine oxidase agrees with those deduced from the nucleotide sequence of the maoA gene. The leader peptide extends over 30 amino acids and has the characteristics of a signal sequence. Primer extension and S1 nuclease mapping of transcripts generated in vivo suggests that the tyramine-induced mRNA starts at a site 62 bases upstream from the ATG initiation codon of the maoC gene. In the putative promoter region, a high degree of similarity to the consensus sequence for the binding site of cyclic AMP receptor protein was found. Thus, the mao region is composed of two cistrons, and the mao operon is regulated by monoamine compounds, glucose, and ammonium ions.

This article has been cited by other articles:

• Autio, K. J., Kastaniotis, A. J., Pospiech, H., Miinalainen, I. J., Schonauer, M. S., Dieckmann, C. L., Hiltunen, J. K. (2008). An ancient genetic link between vertebrate mitochondrial fatty acid synthesis and RNA processing. FASEB J. 22: 569-578 [Abstract] [Full Text]  
• Park, S. J., Lee, S. Y. (2003). Identification and Characterization of a New Enoyl Coenzyme A Hydratase Involved in Biosynthesis of Medium-Chain-Length Polyhydroxyalkanoates in Recombinant Escherichia coli. J. Bacteriol. 185: 5391-5397 [Abstract] [Full Text]  
• Puskarova, A., Ferianc, P., Kormanec, J., Homerova, D., Farewell, A., Nystrom, T. (2002). Regulation of yodA encoding a novel cadmium-induced protein in Escherichia coli. Microbiology 148: 3801-3811 [Abstract] [Full Text]  
• Diaz, E., Ferrandez, A., Prieto, M. A., Garcia, J. L. (2001). Biodegradation of Aromatic Compounds by Escherichia coli. Microbiol. Mol. Biol. Rev. 65: 523-569 [Abstract] [Full Text]  
• Ferrandez, A., Minambres, B., Garcia, B., Olivera, E. R., Luengo, J. M., Garcia, J. L., Diaz, E. (1998). Catabolism of Phenylacetic Acid in Escherichia coli. CHARACTERIZATION OF A NEW AEROBIC HYBRID PATHWAY. J. Biol. Chem. 273: 25974-25986 [Abstract] [Full Text]  
• Olivera, E. R., Minambres, B., Garcia, B., Muniz, C., Moreno, M. A., Ferrandez, A., Diaz, E., Garcia, J. L., Luengo, J. M. (1998). Molecular characterization of the phenylacetic acid catabolic pathway in Pseudomonas putida U: The phenylacetyl-CoA catabolon. Proc. Natl. Acad. Sci. USA 95: 6419-6424 [Abstract] [Full Text]  
• Tipping, A. J., McPherson, M. J. (1995). Cloning and Molecular Analysis of the Pea Seedling Copper Amine Oxidase. J. Biol. Chem. 270: 16939-16946 [Abstract] [Full Text]  
• Choi, Y.-H., Matsuzaki, R., Fukui, T., Shimizu, E., Yorifuji, T., Sato, H., Ozaki, Y., Tanizawa, K. (1995). Copper/Topa Quinone-containing Histamine Oxidase from Arthrobacter globiformis. J. Biol. Chem. 270: 4712-4720 [Abstract] [Full Text]  
• Grogan, G., Roberts, G. A., Bougioukou, D., Turner, N. J., Flitsch, S. L. (2001). The Desymmetrization of Bicyclic beta -Diketones by an Enzymatic Retro-Claisen Reaction. A NEW REACTION OF THE CROTONASE SUPERFAMILY. J. Biol. Chem. 276: 12565-12572 [Abstract] [Full Text]