Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii
Abstract In eukaryotes, the 26S proteasome degrades ubiquitinylated proteins in an ATP-dependent manner. Archaea mediate a form of post-translational modification of proteins termed sampylation that resembles ubiquitinylation. Sampylation was identified in Haloferax volcanii, a moderate halophilic a...
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| Autor*in: |
Prunetti, Laurence [verfasserIn] Reuter, Christopher J. [verfasserIn] Hepowit, Nathaniel L. [verfasserIn] Wu, Yifei [verfasserIn] Barrueto, Luisa [verfasserIn] Miranda, Hugo V. [verfasserIn] Kelly, Karen [verfasserIn] Maupin-Furlow, Julie A. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2013 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Extremophiles - Springer-Verlag, 2001, 18(2013), 2 vom: 17. Dez., Seite 283-293 |
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| Übergeordnetes Werk: |
volume:18 ; year:2013 ; number:2 ; day:17 ; month:12 ; pages:283-293 |
| Links: |
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| DOI / URN: |
10.1007/s00792-013-0615-8 |
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SPR007862334 |
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| 245 | 1 | 0 | |a Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii |
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| 520 | |a Abstract In eukaryotes, the 26S proteasome degrades ubiquitinylated proteins in an ATP-dependent manner. Archaea mediate a form of post-translational modification of proteins termed sampylation that resembles ubiquitinylation. Sampylation was identified in Haloferax volcanii, a moderate halophilic archaeon that synthesizes homologs of 26S proteasome subunits including 20S core particles and regulatory particle triple-A ATPases (Rpt)-like proteasome-associated nucleotidases (PAN-A/1 and PAN-B/2). To determine whether sampylated proteins associate with the Rpt subunit homologs, PAN-A/1 was purified to homogeneity from Hfx. volcanii and analyzed for its subunit stoichiometry, nucleotide-hydrolyzing activity and binding to sampylated protein targets. PAN-A/1 was found to be associated as a dodecamer (630 kDa) with a configuration in TEM suggesting a complex of two stacked hexameric rings. PAN-A/1 had high affinity for ATP (Km of ~0.44 mM) and hydrolyzed this nucleotide with a specific activity of 0.33 ± 0.1 μmol Pi/h per mg protein and maximum at 42 °C. PAN-A1 was stabilized by 2 M salt with a decrease in activity at lower concentrations of salt that correlated with dissociation of the dodecamer into trimers to monomers. Binding of PAN-A/1 to a sampylated protein was demonstrated by modification of a far Western blotting technique (derived from the standard Western blot method to detect protein–protein interaction in vitro) for halophilic proteins. Overall, our results support a model in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling and provide a method for assay of halophilic protein–protein interactions. | ||
| 650 | 4 | |a Archaea |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Protein modification |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Post-translational modification |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a AAA ATPases |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Proteasomes |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Ubiquitylation |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Sampylation |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Reuter, Christopher J. |e verfasserin |4 aut | |
| 700 | 1 | |a Hepowit, Nathaniel L. |e verfasserin |4 aut | |
| 700 | 1 | |a Wu, Yifei |e verfasserin |4 aut | |
| 700 | 1 | |a Barrueto, Luisa |e verfasserin |4 aut | |
| 700 | 1 | |a Miranda, Hugo V. |e verfasserin |4 aut | |
| 700 | 1 | |a Kelly, Karen |e verfasserin |4 aut | |
| 700 | 1 | |a Maupin-Furlow, Julie A. |e verfasserin |4 aut | |
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10.1007/s00792-013-0615-8 doi (DE-627)SPR007862334 (SPR)s00792-013-0615-8-e DE-627 ger DE-627 rakwb eng Prunetti, Laurence verfasserin aut Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In eukaryotes, the 26S proteasome degrades ubiquitinylated proteins in an ATP-dependent manner. Archaea mediate a form of post-translational modification of proteins termed sampylation that resembles ubiquitinylation. Sampylation was identified in Haloferax volcanii, a moderate halophilic archaeon that synthesizes homologs of 26S proteasome subunits including 20S core particles and regulatory particle triple-A ATPases (Rpt)-like proteasome-associated nucleotidases (PAN-A/1 and PAN-B/2). To determine whether sampylated proteins associate with the Rpt subunit homologs, PAN-A/1 was purified to homogeneity from Hfx. volcanii and analyzed for its subunit stoichiometry, nucleotide-hydrolyzing activity and binding to sampylated protein targets. PAN-A/1 was found to be associated as a dodecamer (630 kDa) with a configuration in TEM suggesting a complex of two stacked hexameric rings. PAN-A/1 had high affinity for ATP (Km of ~0.44 mM) and hydrolyzed this nucleotide with a specific activity of 0.33 ± 0.1 μmol Pi/h per mg protein and maximum at 42 °C. PAN-A1 was stabilized by 2 M salt with a decrease in activity at lower concentrations of salt that correlated with dissociation of the dodecamer into trimers to monomers. Binding of PAN-A/1 to a sampylated protein was demonstrated by modification of a far Western blotting technique (derived from the standard Western blot method to detect protein–protein interaction in vitro) for halophilic proteins. Overall, our results support a model in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling and provide a method for assay of halophilic protein–protein interactions. Archaea (dpeaa)DE-He213 Protein modification (dpeaa)DE-He213 Post-translational modification (dpeaa)DE-He213 AAA ATPases (dpeaa)DE-He213 Proteasomes (dpeaa)DE-He213 Ubiquitylation (dpeaa)DE-He213 Sampylation (dpeaa)DE-He213 Reuter, Christopher J. verfasserin aut Hepowit, Nathaniel L. verfasserin aut Wu, Yifei verfasserin aut Barrueto, Luisa verfasserin aut Miranda, Hugo V. verfasserin aut Kelly, Karen verfasserin aut Maupin-Furlow, Julie A. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 18(2013), 2 vom: 17. Dez., Seite 283-293 (DE-627)SPR007852657 nnns volume:18 year:2013 number:2 day:17 month:12 pages:283-293 https://dx.doi.org/10.1007/s00792-013-0615-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 18 2013 2 17 12 283-293 |
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10.1007/s00792-013-0615-8 doi (DE-627)SPR007862334 (SPR)s00792-013-0615-8-e DE-627 ger DE-627 rakwb eng Prunetti, Laurence verfasserin aut Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In eukaryotes, the 26S proteasome degrades ubiquitinylated proteins in an ATP-dependent manner. Archaea mediate a form of post-translational modification of proteins termed sampylation that resembles ubiquitinylation. Sampylation was identified in Haloferax volcanii, a moderate halophilic archaeon that synthesizes homologs of 26S proteasome subunits including 20S core particles and regulatory particle triple-A ATPases (Rpt)-like proteasome-associated nucleotidases (PAN-A/1 and PAN-B/2). To determine whether sampylated proteins associate with the Rpt subunit homologs, PAN-A/1 was purified to homogeneity from Hfx. volcanii and analyzed for its subunit stoichiometry, nucleotide-hydrolyzing activity and binding to sampylated protein targets. PAN-A/1 was found to be associated as a dodecamer (630 kDa) with a configuration in TEM suggesting a complex of two stacked hexameric rings. PAN-A/1 had high affinity for ATP (Km of ~0.44 mM) and hydrolyzed this nucleotide with a specific activity of 0.33 ± 0.1 μmol Pi/h per mg protein and maximum at 42 °C. PAN-A1 was stabilized by 2 M salt with a decrease in activity at lower concentrations of salt that correlated with dissociation of the dodecamer into trimers to monomers. Binding of PAN-A/1 to a sampylated protein was demonstrated by modification of a far Western blotting technique (derived from the standard Western blot method to detect protein–protein interaction in vitro) for halophilic proteins. Overall, our results support a model in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling and provide a method for assay of halophilic protein–protein interactions. Archaea (dpeaa)DE-He213 Protein modification (dpeaa)DE-He213 Post-translational modification (dpeaa)DE-He213 AAA ATPases (dpeaa)DE-He213 Proteasomes (dpeaa)DE-He213 Ubiquitylation (dpeaa)DE-He213 Sampylation (dpeaa)DE-He213 Reuter, Christopher J. verfasserin aut Hepowit, Nathaniel L. verfasserin aut Wu, Yifei verfasserin aut Barrueto, Luisa verfasserin aut Miranda, Hugo V. verfasserin aut Kelly, Karen verfasserin aut Maupin-Furlow, Julie A. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 18(2013), 2 vom: 17. Dez., Seite 283-293 (DE-627)SPR007852657 nnns volume:18 year:2013 number:2 day:17 month:12 pages:283-293 https://dx.doi.org/10.1007/s00792-013-0615-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 18 2013 2 17 12 283-293 |
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10.1007/s00792-013-0615-8 doi (DE-627)SPR007862334 (SPR)s00792-013-0615-8-e DE-627 ger DE-627 rakwb eng Prunetti, Laurence verfasserin aut Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In eukaryotes, the 26S proteasome degrades ubiquitinylated proteins in an ATP-dependent manner. Archaea mediate a form of post-translational modification of proteins termed sampylation that resembles ubiquitinylation. Sampylation was identified in Haloferax volcanii, a moderate halophilic archaeon that synthesizes homologs of 26S proteasome subunits including 20S core particles and regulatory particle triple-A ATPases (Rpt)-like proteasome-associated nucleotidases (PAN-A/1 and PAN-B/2). To determine whether sampylated proteins associate with the Rpt subunit homologs, PAN-A/1 was purified to homogeneity from Hfx. volcanii and analyzed for its subunit stoichiometry, nucleotide-hydrolyzing activity and binding to sampylated protein targets. PAN-A/1 was found to be associated as a dodecamer (630 kDa) with a configuration in TEM suggesting a complex of two stacked hexameric rings. PAN-A/1 had high affinity for ATP (Km of ~0.44 mM) and hydrolyzed this nucleotide with a specific activity of 0.33 ± 0.1 μmol Pi/h per mg protein and maximum at 42 °C. PAN-A1 was stabilized by 2 M salt with a decrease in activity at lower concentrations of salt that correlated with dissociation of the dodecamer into trimers to monomers. Binding of PAN-A/1 to a sampylated protein was demonstrated by modification of a far Western blotting technique (derived from the standard Western blot method to detect protein–protein interaction in vitro) for halophilic proteins. Overall, our results support a model in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling and provide a method for assay of halophilic protein–protein interactions. Archaea (dpeaa)DE-He213 Protein modification (dpeaa)DE-He213 Post-translational modification (dpeaa)DE-He213 AAA ATPases (dpeaa)DE-He213 Proteasomes (dpeaa)DE-He213 Ubiquitylation (dpeaa)DE-He213 Sampylation (dpeaa)DE-He213 Reuter, Christopher J. verfasserin aut Hepowit, Nathaniel L. verfasserin aut Wu, Yifei verfasserin aut Barrueto, Luisa verfasserin aut Miranda, Hugo V. verfasserin aut Kelly, Karen verfasserin aut Maupin-Furlow, Julie A. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 18(2013), 2 vom: 17. Dez., Seite 283-293 (DE-627)SPR007852657 nnns volume:18 year:2013 number:2 day:17 month:12 pages:283-293 https://dx.doi.org/10.1007/s00792-013-0615-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 18 2013 2 17 12 283-293 |
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10.1007/s00792-013-0615-8 doi (DE-627)SPR007862334 (SPR)s00792-013-0615-8-e DE-627 ger DE-627 rakwb eng Prunetti, Laurence verfasserin aut Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In eukaryotes, the 26S proteasome degrades ubiquitinylated proteins in an ATP-dependent manner. Archaea mediate a form of post-translational modification of proteins termed sampylation that resembles ubiquitinylation. Sampylation was identified in Haloferax volcanii, a moderate halophilic archaeon that synthesizes homologs of 26S proteasome subunits including 20S core particles and regulatory particle triple-A ATPases (Rpt)-like proteasome-associated nucleotidases (PAN-A/1 and PAN-B/2). To determine whether sampylated proteins associate with the Rpt subunit homologs, PAN-A/1 was purified to homogeneity from Hfx. volcanii and analyzed for its subunit stoichiometry, nucleotide-hydrolyzing activity and binding to sampylated protein targets. PAN-A/1 was found to be associated as a dodecamer (630 kDa) with a configuration in TEM suggesting a complex of two stacked hexameric rings. PAN-A/1 had high affinity for ATP (Km of ~0.44 mM) and hydrolyzed this nucleotide with a specific activity of 0.33 ± 0.1 μmol Pi/h per mg protein and maximum at 42 °C. PAN-A1 was stabilized by 2 M salt with a decrease in activity at lower concentrations of salt that correlated with dissociation of the dodecamer into trimers to monomers. Binding of PAN-A/1 to a sampylated protein was demonstrated by modification of a far Western blotting technique (derived from the standard Western blot method to detect protein–protein interaction in vitro) for halophilic proteins. Overall, our results support a model in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling and provide a method for assay of halophilic protein–protein interactions. Archaea (dpeaa)DE-He213 Protein modification (dpeaa)DE-He213 Post-translational modification (dpeaa)DE-He213 AAA ATPases (dpeaa)DE-He213 Proteasomes (dpeaa)DE-He213 Ubiquitylation (dpeaa)DE-He213 Sampylation (dpeaa)DE-He213 Reuter, Christopher J. verfasserin aut Hepowit, Nathaniel L. verfasserin aut Wu, Yifei verfasserin aut Barrueto, Luisa verfasserin aut Miranda, Hugo V. verfasserin aut Kelly, Karen verfasserin aut Maupin-Furlow, Julie A. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 18(2013), 2 vom: 17. Dez., Seite 283-293 (DE-627)SPR007852657 nnns volume:18 year:2013 number:2 day:17 month:12 pages:283-293 https://dx.doi.org/10.1007/s00792-013-0615-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 18 2013 2 17 12 283-293 |
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10.1007/s00792-013-0615-8 doi (DE-627)SPR007862334 (SPR)s00792-013-0615-8-e DE-627 ger DE-627 rakwb eng Prunetti, Laurence verfasserin aut Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In eukaryotes, the 26S proteasome degrades ubiquitinylated proteins in an ATP-dependent manner. Archaea mediate a form of post-translational modification of proteins termed sampylation that resembles ubiquitinylation. Sampylation was identified in Haloferax volcanii, a moderate halophilic archaeon that synthesizes homologs of 26S proteasome subunits including 20S core particles and regulatory particle triple-A ATPases (Rpt)-like proteasome-associated nucleotidases (PAN-A/1 and PAN-B/2). To determine whether sampylated proteins associate with the Rpt subunit homologs, PAN-A/1 was purified to homogeneity from Hfx. volcanii and analyzed for its subunit stoichiometry, nucleotide-hydrolyzing activity and binding to sampylated protein targets. PAN-A/1 was found to be associated as a dodecamer (630 kDa) with a configuration in TEM suggesting a complex of two stacked hexameric rings. PAN-A/1 had high affinity for ATP (Km of ~0.44 mM) and hydrolyzed this nucleotide with a specific activity of 0.33 ± 0.1 μmol Pi/h per mg protein and maximum at 42 °C. PAN-A1 was stabilized by 2 M salt with a decrease in activity at lower concentrations of salt that correlated with dissociation of the dodecamer into trimers to monomers. Binding of PAN-A/1 to a sampylated protein was demonstrated by modification of a far Western blotting technique (derived from the standard Western blot method to detect protein–protein interaction in vitro) for halophilic proteins. Overall, our results support a model in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling and provide a method for assay of halophilic protein–protein interactions. Archaea (dpeaa)DE-He213 Protein modification (dpeaa)DE-He213 Post-translational modification (dpeaa)DE-He213 AAA ATPases (dpeaa)DE-He213 Proteasomes (dpeaa)DE-He213 Ubiquitylation (dpeaa)DE-He213 Sampylation (dpeaa)DE-He213 Reuter, Christopher J. verfasserin aut Hepowit, Nathaniel L. verfasserin aut Wu, Yifei verfasserin aut Barrueto, Luisa verfasserin aut Miranda, Hugo V. verfasserin aut Kelly, Karen verfasserin aut Maupin-Furlow, Julie A. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 18(2013), 2 vom: 17. Dez., Seite 283-293 (DE-627)SPR007852657 nnns volume:18 year:2013 number:2 day:17 month:12 pages:283-293 https://dx.doi.org/10.1007/s00792-013-0615-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 18 2013 2 17 12 283-293 |
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Enthalten in Extremophiles 18(2013), 2 vom: 17. Dez., Seite 283-293 volume:18 year:2013 number:2 day:17 month:12 pages:283-293 |
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Enthalten in Extremophiles 18(2013), 2 vom: 17. Dez., Seite 283-293 volume:18 year:2013 number:2 day:17 month:12 pages:283-293 |
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Prunetti, Laurence @@aut@@ Reuter, Christopher J. @@aut@@ Hepowit, Nathaniel L. @@aut@@ Wu, Yifei @@aut@@ Barrueto, Luisa @@aut@@ Miranda, Hugo V. @@aut@@ Kelly, Karen @@aut@@ Maupin-Furlow, Julie A. @@aut@@ |
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Prunetti, Laurence |
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Prunetti, Laurence misc Archaea misc Protein modification misc Post-translational modification misc AAA ATPases misc Proteasomes misc Ubiquitylation misc Sampylation Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii |
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Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii Archaea (dpeaa)DE-He213 Protein modification (dpeaa)DE-He213 Post-translational modification (dpeaa)DE-He213 AAA ATPases (dpeaa)DE-He213 Proteasomes (dpeaa)DE-He213 Ubiquitylation (dpeaa)DE-He213 Sampylation (dpeaa)DE-He213 |
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structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon haloferax volcanii |
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Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii |
| abstract |
Abstract In eukaryotes, the 26S proteasome degrades ubiquitinylated proteins in an ATP-dependent manner. Archaea mediate a form of post-translational modification of proteins termed sampylation that resembles ubiquitinylation. Sampylation was identified in Haloferax volcanii, a moderate halophilic archaeon that synthesizes homologs of 26S proteasome subunits including 20S core particles and regulatory particle triple-A ATPases (Rpt)-like proteasome-associated nucleotidases (PAN-A/1 and PAN-B/2). To determine whether sampylated proteins associate with the Rpt subunit homologs, PAN-A/1 was purified to homogeneity from Hfx. volcanii and analyzed for its subunit stoichiometry, nucleotide-hydrolyzing activity and binding to sampylated protein targets. PAN-A/1 was found to be associated as a dodecamer (630 kDa) with a configuration in TEM suggesting a complex of two stacked hexameric rings. PAN-A/1 had high affinity for ATP (Km of ~0.44 mM) and hydrolyzed this nucleotide with a specific activity of 0.33 ± 0.1 μmol Pi/h per mg protein and maximum at 42 °C. PAN-A1 was stabilized by 2 M salt with a decrease in activity at lower concentrations of salt that correlated with dissociation of the dodecamer into trimers to monomers. Binding of PAN-A/1 to a sampylated protein was demonstrated by modification of a far Western blotting technique (derived from the standard Western blot method to detect protein–protein interaction in vitro) for halophilic proteins. Overall, our results support a model in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling and provide a method for assay of halophilic protein–protein interactions. |
| abstractGer |
Abstract In eukaryotes, the 26S proteasome degrades ubiquitinylated proteins in an ATP-dependent manner. Archaea mediate a form of post-translational modification of proteins termed sampylation that resembles ubiquitinylation. Sampylation was identified in Haloferax volcanii, a moderate halophilic archaeon that synthesizes homologs of 26S proteasome subunits including 20S core particles and regulatory particle triple-A ATPases (Rpt)-like proteasome-associated nucleotidases (PAN-A/1 and PAN-B/2). To determine whether sampylated proteins associate with the Rpt subunit homologs, PAN-A/1 was purified to homogeneity from Hfx. volcanii and analyzed for its subunit stoichiometry, nucleotide-hydrolyzing activity and binding to sampylated protein targets. PAN-A/1 was found to be associated as a dodecamer (630 kDa) with a configuration in TEM suggesting a complex of two stacked hexameric rings. PAN-A/1 had high affinity for ATP (Km of ~0.44 mM) and hydrolyzed this nucleotide with a specific activity of 0.33 ± 0.1 μmol Pi/h per mg protein and maximum at 42 °C. PAN-A1 was stabilized by 2 M salt with a decrease in activity at lower concentrations of salt that correlated with dissociation of the dodecamer into trimers to monomers. Binding of PAN-A/1 to a sampylated protein was demonstrated by modification of a far Western blotting technique (derived from the standard Western blot method to detect protein–protein interaction in vitro) for halophilic proteins. Overall, our results support a model in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling and provide a method for assay of halophilic protein–protein interactions. |
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Abstract In eukaryotes, the 26S proteasome degrades ubiquitinylated proteins in an ATP-dependent manner. Archaea mediate a form of post-translational modification of proteins termed sampylation that resembles ubiquitinylation. Sampylation was identified in Haloferax volcanii, a moderate halophilic archaeon that synthesizes homologs of 26S proteasome subunits including 20S core particles and regulatory particle triple-A ATPases (Rpt)-like proteasome-associated nucleotidases (PAN-A/1 and PAN-B/2). To determine whether sampylated proteins associate with the Rpt subunit homologs, PAN-A/1 was purified to homogeneity from Hfx. volcanii and analyzed for its subunit stoichiometry, nucleotide-hydrolyzing activity and binding to sampylated protein targets. PAN-A/1 was found to be associated as a dodecamer (630 kDa) with a configuration in TEM suggesting a complex of two stacked hexameric rings. PAN-A/1 had high affinity for ATP (Km of ~0.44 mM) and hydrolyzed this nucleotide with a specific activity of 0.33 ± 0.1 μmol Pi/h per mg protein and maximum at 42 °C. PAN-A1 was stabilized by 2 M salt with a decrease in activity at lower concentrations of salt that correlated with dissociation of the dodecamer into trimers to monomers. Binding of PAN-A/1 to a sampylated protein was demonstrated by modification of a far Western blotting technique (derived from the standard Western blot method to detect protein–protein interaction in vitro) for halophilic proteins. Overall, our results support a model in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling and provide a method for assay of halophilic protein–protein interactions. |
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