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Journal of Bacteriology, February 2000, p. 581-588, Vol. 182, No. 3
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Ralstonia eutropha TF93 Is Blocked in Tat-Mediated Protein Export

Michael Bernhard, Bärbel Friedrich, and Roman A. Siddiqui*

Institut für Biologie, Humboldt-Universität zu Berlin, 10115 Berlin, Germany

Received 14 September 1999/Accepted 8 November 1999

Ralstonia eutropha (formerly Alcaligenes eutrophus) TF93 is pleiotropically affected in the translocation of redox enzymes synthesized with an N-terminal signal peptide bearing a twin arginine (S/T-R-R-X-F-L-K) motif. Immunoblot analyses showed that the catalytic subunits of the membrane-bound [NiFe] hydrogenase (MBH) and the molybdenum cofactor-binding periplasmic nitrate reductase (Nap) are mislocalized to the cytoplasm and to the inner membrane, respectively. Moreover, physiological studies showed that the copper-containing nitrous oxide reductase (NosZ) was also not translocated to the periplasm in strain TF93. The cellular localization of enzymes exported by the general secretion system was unaffected. The translocation-arrested MBH and Nap proteins were enzymatically active, suggesting that twin-arginine signal peptide-dependent redox enzymes may have their cofactors inserted prior to transmembrane export. The periplasmic destination of MBH, Nap, and NosZ was restored by heterologous expression of Azotobacter chroococcum tatA mobilized into TF93. tatA encodes a bacterial Hcf106-like protein, a component of a novel protein transport system that has been characterized in thylakoids and shown to translocate folded proteins across the membrane.

* Corresponding author. Mailing address: Institut für Biologie der Humboldt-Universität zu Berlin, Chausseestrasse 117, 10115 Berlin, Germany. Phone: 49-30-2093-8109. Fax: 49-30-2093-8102. E-mail: roman.siddiqui{at}rz.hu-berlin.de.

Journal of Bacteriology, February 2000, p. 581-588, Vol. 182, No. 3
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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