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 Hatchikian, E. C.
Right arrow Articles by Fontecilla-Camps, J. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hatchikian, E. C.
Right arrow Articles by Fontecilla-Camps, J. C.

 Previous Article  |  Next Article 

Journal of Bacteriology, May 1999, p. 2947-2952, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Carboxy-Terminal Processing of the Large Subunit of [Fe] Hydrogenase from Desulfovibrio desulfuricans ATCC 7757

E. Claude Hatchikian,1,* Valérie Magro,1 Nicole Forget,1 Yvain Nicolet,2 and Juan C. Fontecilla-Camps2

Unité de Bioénergétique et Ingéniérie des Protéines, IBSM, CNRS, 13402 Marseilles Cedex 20,1 and Laboratoire de Cristallographie et de Cristallogénèse des Protéines, Institut de Biologie Structurale Jean-Pierre Ebel, CEA-CNRS, 38027 Grenoble Cedex 1,2 France

Received 9 December 1998/Accepted 12 February 1999

hydA and hydB, the genes encoding the large (46-kDa) and small (13.5-kDa) subunits of the periplasmic [Fe] hydrogenase from Desulfovibrio desulfuricans ATCC 7757, have been cloned and sequenced. The deduced amino acid sequence of the genes product showed complete identity to the sequence of the well-characterized [Fe] hydrogenase from the closely related species Desulfovibrio vulgaris Hildenborough (G. Voordouw and S. Brenner, Eur. J. Biochem. 148:515-520, 1985). The data show that in addition to the well-known signal peptide preceding the NH2 terminus of the mature small subunit, the large subunit undergoes a carboxy-terminal processing involving the cleavage of a peptide of 24 residues, in agreement with the recently reported data on the three-dimensional structure of the enzyme (Y. Nicolet, C. Piras, P. Legrand, E. C. Hatchikian, and J. C. Fontecilla-Camps, Structure 7:13-23, 1999). We suggest that this C-terminal processing is involved in the export of the protein to the periplasm.

* Corresponding author. Mailing address: Unité de Bioénergétique et Ingéniérie des Protéines, IBSM, CNRS, 31, Chemin Joseph Aiguier, 13402 Marseilles Cedex 20, France. Phone: 04 91 16 41 45. Fax: 04 91 16 45 78. E-mail: hatch{at}ibsm.cnrs-mrs.fr.

Journal of Bacteriology, May 1999, p. 2947-2952, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Ostberg, Y., Carroll, J. A., Pinne, M., Krum, J. G., Rosa, P., Bergstrom, S. (2004). Pleiotropic Effects of Inactivating a Carboxyl-Terminal Protease, CtpA, in Borrelia burgdorferi. J. Bacteriol. 186: 2074-2084 [Abstract] [Full Text]  
  • Nakanishi, T., Inoue, H., Kitamura, M. (2003). Cloning and Expression of the Superoxide Dismutase Gene from the Obligate Anaerobic Bacterium Desulfovibrio vulgaris (Miyazaki F). J Biochem 133: 387-393 [Abstract] [Full Text]  
  • Noppa, L., Ostberg, Y., Lavrinovicha, M., Bergstrom, S. (2001). P13, an Integral Membrane Protein of Borrelia burgdorferi, Is C-Terminally Processed and Contains Surface-Exposed Domains. Infect. Immun. 69: 3323-3334 [Abstract] [Full Text]  
  • Morelli, X., Czjzek, M., Hatchikian, C. E., Bornet, O., Fontecilla-Camps, J. C., Palma, N. P., Moura, J. J. G., Guerlesquin, F. (2000). Structural Model of the Fe-Hydrogenase/Cytochrome c553 Complex Combining Transverse Relaxation-optimized Spectroscopy Experiments and Soft Docking Calculations. J. Biol. Chem. 275: 23204-23210 [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»