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Journal of Bacteriology, March 1999, p. 1820-1826, Vol. 181, No. 6
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Differential Dependence of Levansucrase and alpha -Amylase Secretion on SecA (Div) during the Exponential Phase of Growth of Bacillus subtilis

Laurence Leloup,1 Arnold J. M. Driessen,2 Roland Freudl,3 Régis Chambert,1 and Marie-Françoise Petit-Glatron1,*

Laboratoire Génétique et Membranes, Institut Jacques Monod, CNRS-Universités Paris 6 et 7, 75251 Paris Cedex 05, France1; Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands2; and Institut für Biotechnologie 1, Forschungszentrum Jülich GmbH, D-52425 Jülich, Germany3

Received 26 October 1998/Accepted 6 January 1999

SecA, the translocation ATPase of the preprotein translocase, accounts for 0.25% of the total protein in a degU32(Hy) Bacillus subtilis strain in logarithmic phase. The SecA level remained constant irrespective of the demand for exoprotein production but dropped about 12-fold during the late stationary phase. Modulation of the level of functional SecA during the exponential phase of growth affected differently the secretion of levansucrase and alpha -amylase overexpressed under the control of the sacB leader region. The level of SecA was reduced in the presence of sodium azide and in the div341 thermosensitive mutant at nonpermissive temperatures. Overproduction of SecA was obtained with a multicopy plasmid bearing secA. The gradual decrease of the SecA level reduced the yield of secreted levansucrase with a concomitant accumulation of unprocessed precursor in the cells, while an increase in the SecA level resulted in an elevation of the production of exocellular levansucrase. In contrast, alpha -amylase secretion was almost unaffected by high concentrations of sodium azide or by very low levels of SecA. Secretion defects were apparent only under conditions of strong SecA deprivation of the cell. These data demonstrate that the alpha -amylase and levansucrase precursors markedly differ in their dependency on SecA for secretion. It is suggested that these precursors differ in their binding affinities for SecA.

* Corresponding author. Mailing address: Institut Jacques Monod, CNRS-Universités Paris 6 et 7, Laboratoire Génétique et Membranes, Tour 43-2, place Jussieu, 75251 Paris Cedex 05-France. Phone: 33 1 44 27 47 19. Fax: 33 1 44 27 59 94. E-mail: glatron{at}ccr.jussieu.fr.

Journal of Bacteriology, March 1999, p. 1820-1826, Vol. 181, No. 6
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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