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Journal of Bacteriology, March 2000, p. 1609-1615, Vol. 182, No. 6
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Evolution of Arginine Biosynthesis in the Bacterial Domain: Novel Gene-Enzyme Relationships from Psychrophilic Moritella Strains (Vibrionaceae) and Evolutionary Significance of N-alpha -Acetyl Ornithinase

Ying Xu,1 Ziyuan Liang,1 Christianne Legrain,2 Hans J. Rüger,3 and Nicolas Glansdorff1,2,*

Laboratory for Genetics and Microbiology, Vrije Universiteit Brussel (VUB), and Department of Microbiology, Flanders Interuniversity Institute for Biotechnology,1 and Jean-Marie Wiame Institute for Microbiological Research,2 B-1070 Brussels, Belgium, and Alfred-Wegener-Institut für Polar- und Meeresforschung, D-27570 Bremerhaven, Germany3

Received 22 September 1999/Accepted 23 December 1999

In the arginine biosynthetic pathway of the vast majority of prokaryotes, the formation of ornithine is catalyzed by an enzyme transferring the acetyl group of N-alpha -acetylornithine to glutamate (ornithine acetyltransferase [OATase]) (argJ encoded). Only two exceptions had been reported---the Enterobacteriaceae and Myxococcus xanthus (members of the gamma  and delta  groups of the class Proteobacteria, respectively)---in which ornithine is produced from N-alpha -acetylornithine by a deacylase, acetylornithinase (AOase) (argE encoded). We have investigated the gene-enzyme relationship in the arginine regulons of two psychrophilic Moritella strains belonging to the Vibrionaceae, a family phylogenetically related to the Enterobacteriaceae. Most of the arg genes were found to be clustered in one continuous sequence divergently transcribed in two wings, argE and argCBFGH(A) ["H(A)" indicates that the argininosuccinase gene consists of a part homologous to known argH sequences and of a 3' extension able to complement an Escherichia coli mutant deficient in the argA gene, encoding N-alpha -acetylglutamate synthetase, the first enzyme committed to the pathway]. Phylogenetic evidence suggests that this new clustering pattern arose in an ancestor common to Vibrionaceae and Enterobacteriaceae, where OATase was lost and replaced by a deacylase. The AOase and ornithine carbamoyltransferase of these psychrophilic strains both display distinctly cold-adapted activity profiles, providing the first cold-active examples of such enzymes.

* Corresponding author. Mailing address: Laboratory for Genetics and Microbiology, Vrije Universiteit Brussel (VUB), and Department of Microbiology, Flanders Interuniversity Institute for Biotechnology, 1, E. Gryson Ave., B-1070 Brussels, Belgium. Phone: 32-2-526 72 75. Fax: 32-2-526 72 73. E-mail: ceriair{at}ulb.ac.be.

Journal of Bacteriology, March 2000, p. 1609-1615, Vol. 182, No. 6
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Xu, Y., Labedan, B., Glansdorff, N. (2007). Surprising Arginine Biosynthesis: a Reappraisal of the Enzymology and Evolution of the Pathway in Microorganisms. Microbiol. Mol. Biol. Rev. 71: 36-47 [Abstract] [Full Text]  
  • Errey, J. C., Blanchard, J. S. (2005). Functional Characterization of a Novel ArgA from Mycobacterium tuberculosis. J. Bacteriol. 187: 3039-3044 [Abstract] [Full Text]  
  • Xu, Y., Feller, G., Gerday, C., Glansdorff, N. (2003). Moritella Cold-Active Dihydrofolate Reductase: Are There Natural Limits to Optimization of Catalytic Efficiency at Low Temperature?. J. Bacteriol. 185: 5519-5526 [Abstract] [Full Text]  
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