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M210762200v1
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Papers In Press, published online ahead of print February 3, 2003
J. Biol. Chem, 10.1074/jbc.M210762200
Submitted on October 22, 2002
Revised on January 30, 2003
Accepted on February 3, 2003

Post-translational secretion of fusion proteins in the halophilic archaeon Haloferax volcanii

Vered Irihimovitch and Jerry Eichler

Life Sciences, Ben Gurion University, Beersheva 84105

Corresponding Author: jeichler{at}bgumail.bgu.ac.il

Whereas protein secretion occurs post-translationally in Bacteria and is mainly a co-translational event in Eukarya, the relationship between the translation and translocation of secreted proteins in Archaea is not known. To address this question, the signal peptide-encoding region of the surface layer glycoprotein gene from the haloarchaeon Haloferax volcanii was fused to either the cellulose-binding domain of the Clostridium thermocellum cellulosome or to the cytoplasmic enzyme dihydrofolate reductase from Haloferax volcanii. Signal peptide-cleaved, mature versions of both the cellulose-binding domain and dihydrofolate reductase could be detected in the growth medium of transformed Haloferax volcanii cells. Immunoblot analysis, however, revealed the presence of full-length, signal peptide-bearing forms of both proteins inside the cytoplasm of the transformed cells. Proteinase accessibility assays confirmed that the presence of cell-associated, signal peptide-bearing proteins was not due to medium contamination. Moreover, the pulse-radiolabeled signal peptide-cellulose-binding domain chimera could be chased from the cytoplasm into the growth medium even following treatment with anisomycin, an antibiotic inhibitor of haloarchaeal protein translation. Thus, these results provide evidence that in Archaea, at least some secreted proteins are first synthesized inside the cell and only then translocated across the plasma membrane into the medium.


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