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.
Unité de Bioénergétique et
Ingéniérie des Protéines,
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.
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