This Article Full Text 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 Belfaiza, J. Articles by Saint Girons, I. Search for Related Content PubMed PubMed Citation Articles by Belfaiza, J. Articles by Saint Girons, I.

 Previous Article  |  Next Article 

J. Bacteriol., Jan 1998, 250-255, Vol 180, No. 2
Copyright © 1998, American Society for Microbiology

Direct sulfhydrylation for methionine biosynthesis in Leptospira meyeri [In Process Citation]

J Belfaiza, A Martel, D Margarita and I Saint Girons
Faculte des Sciences d'El-Jadida, Universite Chouaib Doukkali, El- Jadida, Morocco.

A gene library of the Leptospira meyeri serovar semaranga strain Veldrat S.173 DNA has been constructed in a mobilizable cosmid with inserts of up to 40 kb. It was demonstrated that a Leptospira DNA fragment carrying metY complemented Escherichia coli strains carrying mutations in metB. The latter gene encodes cystathionine gamma- synthase, an enzyme which catalyzes the second step of the methionine biosynthetic pathway. The metY gene is 1,304 bp long and encodes a 443- amino-acid protein with a molecular mass of 45 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The deduced amino acid sequence of the Leptospira metY product has a high degree of similarity to those of O-acetylhomoserine sulfhydrylases from Aspergillus nidulans and Saccharomyces cerevisiae. A lower degree of sequence similarity was also found with bacterial cystathionine gamma- synthase. The L. meyeri metY gene was overexpressed under the control of the T7 promoter. MetY exhibits an O-acetylhomoserine sulfhydrylase activity. Genetic, enzymatic, and physiological studies reveal that the transsulfuration pathway via cystathionine does not exist in L. meyeri, in contrast to the situation found for fungi and some bacteria. Our results indicate, therefore, that the L. meyeri MetY enzyme is able to perform direct sulfhydrylation for methionine biosynthesis by using O- acetylhomoserine as a substrate.

This article has been cited by other articles:

• Rodionov, D. A., Vitreschak, A. G., Mironov, A. A., Gelfand, M. S. (2004). Comparative genomics of the methionine metabolism in Gram-positive bacteria: a variety of regulatory systems. Nucleic Acids Res 32: 3340-3353 [Abstract] [Full Text]  
• Hacham, Y., Gophna, U., Amir, R. (2003). In Vivo Analysis of Various Substrates Utilized by Cystathionine {gamma}-Synthase and O-Acetylhomoserine Sulfhydrylase in Methionine Biosynthesis. Mol Biol Evol 20: 1513-1520 [Abstract] [Full Text]  
• Bauby, H., Saint Girons, I., Picardeau, M. (2003). Construction and complementation of the first auxotrophic mutant in the spirochaete Leptospira meyeri. Microbiology 149: 689-693 [Abstract] [Full Text]  
• Hwang, B.-J., Yeom, H.-J., Kim, Y., Lee, H.-S. (2002). Corynebacterium glutamicum Utilizes both Transsulfuration and Direct Sulfhydrylation Pathways for Methionine Biosynthesis. J. Bacteriol. 184: 1277-1286 [Abstract] [Full Text]  
• Auger, S., Yuen, W. H., Danchin, A., Martin-Verstraete, I. (2002). The metIC operon involved in methionine biosynthesis in Bacillus subtilis is controlled by transcription antitermination. Microbiology 148: 507-518 [Abstract] [Full Text]  
• Brenot, A., Trott, D., Girons, I. S., Zuerner, R. (2001). Penicillin-Binding Proteins in Leptospira interrogans. Antimicrob. Agents Chemother. 45: 870-877 [Abstract] [Full Text]  
• Pradel, E., Guiso, N., Menozzi, F. D., Locht, C. (2000). Bordetella pertussis TonB, a Bvg-Independent Virulence Determinant. Infect. Immun. 68: 1919-1927 [Abstract] [Full Text]  
• Vermeij, P., Kertesz, M. A. (1999). Pathways of Assimilative Sulfur Metabolism in Pseudomonas putida. J. Bacteriol. 181: 5833-5837 [Abstract] [Full Text]