This Article Full Text Full Text (PDF) Other Versions of this Article: JB.01273-06v1 189/1/187    most recent 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 Hullo, M.-F. Articles by Martin-Verstraete, I. Search for Related Content PubMed PubMed Citation Articles by Hullo, M.-F. Articles by Martin-Verstraete, I.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2007, p. 187-197, Vol. 189, No. 1
0021-9193/07/$08.00+0     doi:10.1128/JB.01273-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Conversion of Methionine to Cysteine in Bacillus subtilis and Its Regulation

Marie-Françoise Hullo,^1, Sandrine Auger,^1,, Olga Soutourina,^1,2 Octavian Barzu,¹ Mireille Yvon,³ Antoine Danchin,¹ and Isabelle Martin-Verstraete^1,2*

Unité de Génétique des Génomes Bactériens, Institut Pasteur, URA CNRS 2171, 28 Rue du Docteur Roux, 75724 Paris Cedex 15, France,¹ UFR de Biochimie, Université Paris 7-Denis Diderot, 2 Place Jussieu, 75251 Paris, France,² Unité de Biochimie Bactérienne (BIOBAC), INRA, 78352 Jouy-en-Josas, France³

Received 11 August 2006/ Accepted 11 October 2006

Bacillus subtilis can use methionine as the sole sulfur source, indicating an efficient conversion of methionine to cysteine. To characterize this pathway, the enzymatic activities of CysK, YrhA and YrhB purified in Escherichia coli were tested. Both CysK and YrhA have an O-acetylserine-thiol-lyase activity, but YrhA was 75-fold less active than CysK. An atypical cystathionine ß-synthase activity using O-acetylserine and homocysteine as substrates was observed for YrhA but not for CysK. The YrhB protein had both cystathionine lyase and homocysteine -lyase activities in vitro. Due to their activity, we propose that YrhA and YrhB should be renamed MccA and MccB for methionine-to-cysteine conversion. Mutants inactivated for cysK or yrhB grew similarly to the wild-type strain in the presence of methionine. In contrast, the growth of an yrhA mutant or a luxS mutant, inactivated for the S-ribosyl-homocysteinase step of the S-adenosylmethionine recycling pathway, was strongly reduced with methionine, whereas a yrhA cysK or cysE mutant did not grow at all under the same conditions. The yrhB and yrhA genes form an operon together with yrrT, mtnN, and yrhC. The expression of the yrrT operon was repressed in the presence of sulfate or cysteine. Both purified CysK and CymR, the global repressor of cysteine metabolism, were required to observe the formation of a protein-DNA complex with the yrrT promoter region in gel-shift experiments. The addition of O-acetyl-serine prevented the formation of this protein-DNA complex.

Published ahead of print on 20 October 2006.

M.-F.H. and S.A. contributed equally to this study.

Present address: Unité de Génétique Microbienne, INRA, Domaine de Vilvert, 78352 Jouy en Josas, France.

This article has been cited by other articles:

• 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 0: gkn601v1-gkn601 [Abstract] [Full Text]  
• Paige, C., Reid, S. D., Hanna, P. C., Claiborne, A. (2008). The Type III Pantothenate Kinase Encoded by coaX Is Essential for Growth of Bacillus anthracis. J. Bacteriol. 190: 6271-6275 [Abstract] [Full Text]  
• Liu, M., Nauta, A., Francke, C., Siezen, R. J. (2008). Comparative Genomics of Enzymes in Flavor-Forming Pathways from Amino Acids in Lactic Acid Bacteria. Appl. Environ. Microbiol. 74: 4590-4600 [Full Text]  
• Moller, M. C., Hederstedt, L. (2008). Extracytoplasmic Processes Impaired by Inactivation of trxA (Thioredoxin Gene) in Bacillus subtilis. J. Bacteriol. 190: 4660-4665 [Abstract] [Full Text]  
• Hochgrafe, F., Mostertz, J., Pother, D.-C., Becher, D., Helmann, J. D., Hecker, M. (2007). S-Cysteinylation Is a General Mechanism for Thiol Protection of Bacillus subtilis Proteins after Oxidative Stress. J. Biol. Chem. 282: 25981-25985 [Abstract] [Full Text]  
• Mechold, U., Fang, G., Ngo, S., Ogryzko, V., Danchin, A. (2007). YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity. Nucleic Acids Res 35: 4552-4561 [Abstract] [Full Text]