This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vermeij, P.
Right arrow Articles by Kertesz, M. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vermeij, P.
Right arrow Articles by Kertesz, M. A.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 1999, p. 5833-5837, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Pathways of Assimilative Sulfur Metabolism in Pseudomonas putida

Paul Vermeij and Michael A. Kertesz*

Institute of Microbiology, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092 Zürich, Switzerland

Received 17 May 1999/Accepted 12 July 1999

Cysteine and methionine biosynthesis was studied in Pseudomonas putida S-313 and Pseudomonas aeruginosa PAO1. Both these organisms used direct sulfhydrylation of O-succinylhomoserine for the synthesis of methionine but also contained substantial levels of O-acetylserine sulfhydrylase (cysteine synthase) activity. The enzymes of the transsulfuration pathway (cystathionine gamma -synthase and cystathionine beta -lyase) were expressed at low levels in both pseudomonads but were strongly upregulated during growth with cysteine as the sole sulfur source. In P. aeruginosa, the reverse transsulfuration pathway between homocysteine and cysteine, with cystathionine as the intermediate, allows P. aeruginosa to grow rapidly with methionine as the sole sulfur source. P. putida S-313 also grew well with methionine as the sulfur source, but no cystathionine gamma -lyase, the key enzyme of the reverse transsulfuration pathway, was found in this species. In the absence of the reverse transsulfuration pathway, P. putida desulfurized methionine by the conversion of methionine to methanethiol, catalyzed by methionine gamma -lyase, which was upregulated under these conditions. A transposon mutant of P. putida that was defective in the alkanesulfonatase locus (ssuD) was unable to grow with either methanesulfonate or methionine as the sulfur source. We therefore propose that in P. putida methionine is converted to methanethiol and then oxidized to methanesulfonate. The sulfonate is then desulfonated by alkanesulfonatase to release sulfite for reassimilation into cysteine.

* Corresponding author. Mailing address: Mikrobiologisches Institut, ETH-Zentrum/LFV, CH-8092 Zürich, Switzerland. Phone: 41 1 632 33 57. Fax: 41 1 632 11 48. E-mail: kertesz{at}micro.biol.ethz.ch.

Journal of Bacteriology, September 1999, p. 5833-5837, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Lee, S.-M., Hwang, B.-J., Kim, Y., Lee, H.-S. (2009). The cmaR gene of Corynebacterium ammoniagenes performs a novel regulatory role in the metabolism of sulfur-containing amino acids. Microbiology 155: 1878-1889 [Abstract] [Full Text]  
  • Lo, R., Turner, M. S., Barry, D. G., Sreekumar, R., Walsh, T. P., Giffard, P. M. (2009). Cystathionine {gamma}-Lyase Is a Component of Cystine-Mediated Oxidative Defense in Lactobacillus reuteri BR11. J. Bacteriol. 191: 1827-1837 [Abstract] [Full Text]  
  • Andre, G., Even, S., Putzer, H., Burguiere, P., Croux, C., Danchin, A., Martin-Verstraete, I., Soutourina, O. (2008). S-box and T-box riboswitches and antisense RNA control a sulfur metabolic operon of Clostridium acetobutylicum. Nucleic Acids Res 36: 5955-5969 [Abstract] [Full Text]  
  • Kouzuma, A., Endoh, T., Omori, T., Nojiri, H., Yamane, H., Habe, H. (2008). Transcription Factors CysB and SfnR Constitute the Hierarchical Regulatory System for the Sulfate Starvation Response in Pseudomonas putida. J. Bacteriol. 190: 4521-4531 [Abstract] [Full Text]  
  • Habe, H., Kouzuma, A., Endoh, T., Omori, T., Yamane, H., Nojiri, H. (2007). Transcriptional regulation of the sulfate-starvation-induced gene sfnA by a {sigma}54-dependent activator of Pseudomonas putida. Microbiology 153: 3091-3098 [Abstract] [Full Text]  
  • Kudou, D., Misaki, S., Yamashita, M., Tamura, T., Takakura, T., Yoshioka, T., Yagi, S., Hoffman, R. M, Takimoto, A., Esaki, N., Inagaki, K. (2007). Structure of the Antitumour Enzyme L-Methionine {gamma}-Lyase from Pseudomonas putida at 1.8 A Resolution. J Biochem 141: 535-544 [Abstract] [Full Text]  
  • Goyer, A., Collakova, E., Shachar-Hill, Y., Hanson, A. D. (2007). Functional Characterization of a Methionine {gamma}-Lyase in Arabidopsis and its Implication in an Alternative to the Reverse Trans-sulfuration Pathway. Plant Cell Physiol 48: 232-242 [Abstract] [Full Text]  
  • Hullo, M.-F., Auger, S., Soutourina, O., Barzu, O., Yvon, M., Danchin, A., Martin-Verstraete, I. (2007). Conversion of Methionine to Cysteine in Bacillus subtilis and Its Regulation. J. Bacteriol. 189: 187-197 [Abstract] [Full Text]  
  • Seiflein, T. A., Lawrence, J. G. (2006). Two Transsulfurylation Pathways in Klebsiella pneumoniae.. J. Bacteriol. 188: 5762-5774 [Abstract] [Full Text]  
  • Reva, O. N., Weinel, C., Weinel, M., Bohm, K., Stjepandic, D., Hoheisel, J. D., Tummler, B. (2006). Functional Genomics of Stress Response in Pseudomonas putida KT2440. J. Bacteriol. 188: 4079-4092 [Abstract] [Full Text]  
  • Farmer, K. L., Thomas, M. S. (2004). Isolation and Characterization of Burkholderia cenocepacia Mutants Deficient in Pyochelin Production: Pyochelin Biosynthesis Is Sensitive to Sulfur Availability. J. Bacteriol. 186: 270-277 [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]  
  • Seiflein, T. A., Lawrence, J. G. (2001). Methionine-to-Cysteine Recycling in Klebsiella aerogenes. J. Bacteriol. 183: 336-346 [Abstract] [Full Text]  
  • Kahnert, A., Vermeij, P., Wietek, C., James, P., Leisinger, T., Kertesz, M. A. (2000). The ssu Locus Plays a Key Role in Organosulfur Metabolism in Pseudomonas putida S-313. J. Bacteriol. 182: 2869-2878 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»