Schmid, G. and Mathiesen, G. and Arntzen, M. O. and Eijsink, V. G. H. and Thomm, M. (2013) Experimental and computational analysis of the secretome of the hyperthermophilic archaeon Pyrococcus furiosus. EXTREMOPHILES, 17 (6). pp. 921-930. ISSN 1431-0651, 1433-4909
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Although Pyrococcus furiosus is one of the best studied hyperthermophilic archaea, to date no experimental investigation of the extent of protein secretion has been performed. We describe experimental verification of the extracellular proteome of P. furiosus grown on starch. LC-MS/MS-based analysis of culture supernatants led to the identification of 58 proteins. Fifteen of these proteins had a putative N-terminal signal peptide (SP), tagging the proteins for translocation across the membrane. The detected proteins with predicted SPs and known function were almost exclusively involved in important extracellular functions, like substrate degradation or transport. Most of the 43 proteins without predicted N-terminal signal sequences are known to have intracellular functions, mainly (70 %) related to intracellular metabolism. In silico analyses indicated that the genome of P. furiosus encodes 145 proteins with N-terminal SPs, including 21 putative lipoproteins and 17 with a class III peptide. From these we identified 15 (10 %; 7 SPI, 3 SPIII and 5 lipoproteins) under the specific growth conditions of this study. The putative lipoprotein signal peptides have a unique sequence motif, distinct from the motifs in bacteria and other archaeal orders.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SIGNAL PEPTIDES; BACTERIAL LIPOPROTEINS; SERINE-PROTEASE; PROTEINS; IDENTIFICATION; PREDICTION; COMPONENTS; PROTEOMICS; PYROLYSIN; VESICLES; Pyrococcus; Exoproteome; Exoenzymes; Signal peptides; Archaea; Lipoprotein |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie > Prof. Dr. Michael Thomm |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 26 Mar 2020 12:52 |
| Last Modified: | 26 Mar 2020 12:52 |
| URI: | https://pred.uni-regensburg.de/id/eprint/15787 |
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