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Journal of Bacteriology, March 2001, p. 1881-1890, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.1881-1890.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Quantitation of the Capacity of the Secretion Apparatus and Requirement for PrsA in Growth and Secretion of alpha -Amylase in Bacillus subtilis

Marika Vitikainen, Tiina Pummi, Ulla Airaksinen,dagger Eva Wahlström, Hongyan Wu,Dagger Matti Sarvas, and Vesa P. Kontinen*

Vaccine Development Laboratory, National Public Health Institute, FIN-00300 Helsinki, Finland

Received 18 September 2000/Accepted 6 December 2000

Regulated expression of AmyQ alpha -amylase of Bacillus amyloliquefaciens was used to examine the capacity of the protein secretion apparatus of B. subtilis. One B. subtilis cell was found to secrete maximally 10 fg of AmyQ per h. The signal peptidase SipT limits the rate of processing of the signal peptide. Another limit is set by PrsA lipoprotein. The wild-type level of PrsA was found to be 2 × 104 molecules per cell. Decreasing the cellular level of PrsA did not decrease the capacity of the protein translocation or signal peptide processing steps but dramatically affected secretion in a posttranslocational step. There was a linear correlation between the number of cellular PrsA molecules and the number of secreted AmyQ molecules over a wide range of prsA and amyQ expression levels. Significantly, even when amyQ was expressed at low levels, overproduction of PrsA enhanced its secretion. The finding is consistent with a reversible interaction between PrsA and AmyQ. The high cellular level of PrsA suggests a chaperone-like function. PrsA was also found to be essential for the viability of B. subtilis. Drastic depletion of PrsA resulted in altered cellular morphology and ultimately in cell death.

* Corresponding author. Vaccine Development Laboratory, National Public Health Institute, Mannerheimintie 166, FIN-00300 Helsinki, Finland. Phone: 358-9-47448562. Fax: 358-9-47448347. E-mail: Vesa.Kontinen{at}ktl.fi.

dagger Present address: Laboratory of Bioprocess Engineering, Helsinki University of Technology, FIN-02015 Espoo, Finland.

Dagger Present address: Medicity Research Laboratory, University of Turku and National Public Health Institute, FIN-20520 Turku, Finland.

Journal of Bacteriology, March 2001, p. 1881-1890, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.1881-1890.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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