Experimental and computational analysis of the secretome of the hyperthermophilic archaeon Pyrococcus furiosus
Abstract 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...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Schmid, G. [verfasserIn] Mathiesen, G. [verfasserIn] Arntzen, M. O. [verfasserIn] Eijsink, V. G. H. [verfasserIn] Thomm, M. [verfasserIn] |
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E-Artikel |
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Englisch |
| Erschienen: |
2013 |
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Enthalten in: Extremophiles - Springer-Verlag, 2001, 17(2013), 6 vom: 27. Aug., Seite 921-930 |
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volume:17 ; year:2013 ; number:6 ; day:27 ; month:08 ; pages:921-930 |
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10.1007/s00792-013-0574-0 |
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| 520 | |a Abstract 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. | ||
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| 700 | 1 | |a Thomm, M. |e verfasserin |4 aut | |
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10.1007/s00792-013-0574-0 doi (DE-627)SPR007861877 (SPR)s00792-013-0574-0-e DE-627 ger DE-627 rakwb eng Schmid, G. verfasserin aut Experimental and computational analysis of the secretome of the hyperthermophilic archaeon Pyrococcus furiosus 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 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. Exoproteome (dpeaa)DE-He213 Exoenzymes (dpeaa)DE-He213 Signal peptides (dpeaa)DE-He213 Archaea (dpeaa)DE-He213 Lipoprotein (dpeaa)DE-He213 Mathiesen, G. verfasserin aut Arntzen, M. O. verfasserin aut Eijsink, V. G. H. verfasserin aut Thomm, M. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 17(2013), 6 vom: 27. Aug., Seite 921-930 (DE-627)SPR007852657 nnns volume:17 year:2013 number:6 day:27 month:08 pages:921-930 https://dx.doi.org/10.1007/s00792-013-0574-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 17 2013 6 27 08 921-930 |
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10.1007/s00792-013-0574-0 doi (DE-627)SPR007861877 (SPR)s00792-013-0574-0-e DE-627 ger DE-627 rakwb eng Schmid, G. verfasserin aut Experimental and computational analysis of the secretome of the hyperthermophilic archaeon Pyrococcus furiosus 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 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. Exoproteome (dpeaa)DE-He213 Exoenzymes (dpeaa)DE-He213 Signal peptides (dpeaa)DE-He213 Archaea (dpeaa)DE-He213 Lipoprotein (dpeaa)DE-He213 Mathiesen, G. verfasserin aut Arntzen, M. O. verfasserin aut Eijsink, V. G. H. verfasserin aut Thomm, M. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 17(2013), 6 vom: 27. Aug., Seite 921-930 (DE-627)SPR007852657 nnns volume:17 year:2013 number:6 day:27 month:08 pages:921-930 https://dx.doi.org/10.1007/s00792-013-0574-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 17 2013 6 27 08 921-930 |
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10.1007/s00792-013-0574-0 doi (DE-627)SPR007861877 (SPR)s00792-013-0574-0-e DE-627 ger DE-627 rakwb eng Schmid, G. verfasserin aut Experimental and computational analysis of the secretome of the hyperthermophilic archaeon Pyrococcus furiosus 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 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. Exoproteome (dpeaa)DE-He213 Exoenzymes (dpeaa)DE-He213 Signal peptides (dpeaa)DE-He213 Archaea (dpeaa)DE-He213 Lipoprotein (dpeaa)DE-He213 Mathiesen, G. verfasserin aut Arntzen, M. O. verfasserin aut Eijsink, V. G. H. verfasserin aut Thomm, M. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 17(2013), 6 vom: 27. Aug., Seite 921-930 (DE-627)SPR007852657 nnns volume:17 year:2013 number:6 day:27 month:08 pages:921-930 https://dx.doi.org/10.1007/s00792-013-0574-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 17 2013 6 27 08 921-930 |
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10.1007/s00792-013-0574-0 doi (DE-627)SPR007861877 (SPR)s00792-013-0574-0-e DE-627 ger DE-627 rakwb eng Schmid, G. verfasserin aut Experimental and computational analysis of the secretome of the hyperthermophilic archaeon Pyrococcus furiosus 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 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. Exoproteome (dpeaa)DE-He213 Exoenzymes (dpeaa)DE-He213 Signal peptides (dpeaa)DE-He213 Archaea (dpeaa)DE-He213 Lipoprotein (dpeaa)DE-He213 Mathiesen, G. verfasserin aut Arntzen, M. O. verfasserin aut Eijsink, V. G. H. verfasserin aut Thomm, M. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 17(2013), 6 vom: 27. Aug., Seite 921-930 (DE-627)SPR007852657 nnns volume:17 year:2013 number:6 day:27 month:08 pages:921-930 https://dx.doi.org/10.1007/s00792-013-0574-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 17 2013 6 27 08 921-930 |
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10.1007/s00792-013-0574-0 doi (DE-627)SPR007861877 (SPR)s00792-013-0574-0-e DE-627 ger DE-627 rakwb eng Schmid, G. verfasserin aut Experimental and computational analysis of the secretome of the hyperthermophilic archaeon Pyrococcus furiosus 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 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. Exoproteome (dpeaa)DE-He213 Exoenzymes (dpeaa)DE-He213 Signal peptides (dpeaa)DE-He213 Archaea (dpeaa)DE-He213 Lipoprotein (dpeaa)DE-He213 Mathiesen, G. verfasserin aut Arntzen, M. O. verfasserin aut Eijsink, V. G. H. verfasserin aut Thomm, M. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 17(2013), 6 vom: 27. Aug., Seite 921-930 (DE-627)SPR007852657 nnns volume:17 year:2013 number:6 day:27 month:08 pages:921-930 https://dx.doi.org/10.1007/s00792-013-0574-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 17 2013 6 27 08 921-930 |
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Experimental and computational analysis of the secretome of the hyperthermophilic archaeon Pyrococcus furiosus |
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Abstract 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. |
| abstractGer |
Abstract 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. |
| abstract_unstemmed |
Abstract 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. |
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| title_short |
Experimental and computational analysis of the secretome of the hyperthermophilic archaeon Pyrococcus furiosus |
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https://dx.doi.org/10.1007/s00792-013-0574-0 |
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Mathiesen, G. Arntzen, M. O. Eijsink, V. G. H. Thomm, M. |
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Mathiesen, G. Arntzen, M. O. Eijsink, V. G. H. Thomm, M. |
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2024-07-03T15:43:34.341Z |
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