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...
Ausführliche Beschreibung
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] |
---|
Format: |
E-Artikel |
---|---|
Sprache: |
Englisch |
Erschienen: |
2013 |
---|
Schlagwörter: |
---|
Übergeordnetes Werk: |
Enthalten in: Extremophiles - Springer-Verlag, 2001, 18(2013), 2 vom: 17. Dez., Seite 283-293 |
---|---|
Übergeordnetes Werk: |
volume:18 ; year:2013 ; number:2 ; day:17 ; month:12 ; pages:283-293 |
Links: |
---|
DOI / URN: |
10.1007/s00792-013-0615-8 |
---|
Katalog-ID: |
SPR007862334 |
---|
LEADER | 01000caa a22002652 4500 | ||
---|---|---|---|
001 | SPR007862334 | ||
003 | DE-627 | ||
005 | 20201124022546.0 | ||
007 | cr uuu---uuuuu | ||
008 | 201005s2013 xx |||||o 00| ||eng c | ||
024 | 7 | |a 10.1007/s00792-013-0615-8 |2 doi | |
035 | |a (DE-627)SPR007862334 | ||
035 | |a (SPR)s00792-013-0615-8-e | ||
040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
041 | |a eng | ||
100 | 1 | |a Prunetti, Laurence |e verfasserin |4 aut | |
245 | 1 | 0 | |a Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii |
264 | 1 | |c 2013 | |
336 | |a Text |b txt |2 rdacontent | ||
337 | |a Computermedien |b c |2 rdamedia | ||
338 | |a Online-Ressource |b cr |2 rdacarrier | ||
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 | |
773 | 0 | 8 | |i Enthalten in |t Extremophiles |d Springer-Verlag, 2001 |g 18(2013), 2 vom: 17. Dez., Seite 283-293 |w (DE-627)SPR007852657 |7 nnns |
773 | 1 | 8 | |g volume:18 |g year:2013 |g number:2 |g day:17 |g month:12 |g pages:283-293 |
856 | 4 | 0 | |u https://dx.doi.org/10.1007/s00792-013-0615-8 |z lizenzpflichtig |3 Volltext |
912 | |a GBV_USEFLAG_A | ||
912 | |a SYSFLAG_A | ||
912 | |a GBV_SPRINGER | ||
951 | |a AR | ||
952 | |d 18 |j 2013 |e 2 |b 17 |c 12 |h 283-293 |
author_variant |
l p lp c j r cj cjr n l h nl nlh y w yw l b lb h v m hv hvm k k kk j a m f jam jamf |
---|---|
matchkey_str |
prunettilaurencereuterchristopherjhepowi:2013----:tutrlnbohmclrprisfnxrmsllvnpoesmatvtnncetds |
hierarchy_sort_str |
2013 |
publishDate |
2013 |
allfields |
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 |
spelling |
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 |
allfields_unstemmed |
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 |
allfieldsGer |
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 |
allfieldsSound |
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 |
language |
English |
source |
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 |
sourceStr |
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 |
format_phy_str_mv |
Article |
institution |
findex.gbv.de |
topic_facet |
Archaea Protein modification Post-translational modification AAA ATPases Proteasomes Ubiquitylation Sampylation |
isfreeaccess_bool |
false |
container_title |
Extremophiles |
authorswithroles_txt_mv |
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@@ |
publishDateDaySort_date |
2013-12-17T00:00:00Z |
hierarchy_top_id |
SPR007852657 |
id |
SPR007862334 |
language_de |
englisch |
fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR007862334</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20201124022546.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201005s2013 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s00792-013-0615-8</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR007862334</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s00792-013-0615-8-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Prunetti, Laurence</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2013</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="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.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Archaea</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein modification</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Post-translational modification</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">AAA ATPases</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Proteasomes</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Ubiquitylation</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Sampylation</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Reuter, Christopher J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hepowit, Nathaniel L.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wu, Yifei</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Barrueto, Luisa</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Miranda, Hugo V.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kelly, Karen</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Maupin-Furlow, Julie A.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Extremophiles</subfield><subfield code="d">Springer-Verlag, 2001</subfield><subfield code="g">18(2013), 2 vom: 17. Dez., Seite 283-293</subfield><subfield code="w">(DE-627)SPR007852657</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:18</subfield><subfield code="g">year:2013</subfield><subfield code="g">number:2</subfield><subfield code="g">day:17</subfield><subfield code="g">month:12</subfield><subfield code="g">pages:283-293</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://dx.doi.org/10.1007/s00792-013-0615-8</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_SPRINGER</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">18</subfield><subfield code="j">2013</subfield><subfield code="e">2</subfield><subfield code="b">17</subfield><subfield code="c">12</subfield><subfield code="h">283-293</subfield></datafield></record></collection>
|
author |
Prunetti, Laurence |
spellingShingle |
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 |
authorStr |
Prunetti, Laurence |
ppnlink_with_tag_str_mv |
@@773@@(DE-627)SPR007852657 |
format |
electronic Article |
delete_txt_mv |
keep |
author_role |
aut aut aut aut aut aut aut aut |
collection |
springer |
remote_str |
true |
illustrated |
Not Illustrated |
topic_title |
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 |
topic |
misc Archaea misc Protein modification misc Post-translational modification misc AAA ATPases misc Proteasomes misc Ubiquitylation misc Sampylation |
topic_unstemmed |
misc Archaea misc Protein modification misc Post-translational modification misc AAA ATPases misc Proteasomes misc Ubiquitylation misc Sampylation |
topic_browse |
misc Archaea misc Protein modification misc Post-translational modification misc AAA ATPases misc Proteasomes misc Ubiquitylation misc Sampylation |
format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
format_main_str_mv |
Text Zeitschrift/Artikel |
carriertype_str_mv |
cr |
hierarchy_parent_title |
Extremophiles |
hierarchy_parent_id |
SPR007852657 |
hierarchy_top_title |
Extremophiles |
isfreeaccess_txt |
false |
familylinks_str_mv |
(DE-627)SPR007852657 |
title |
Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii |
ctrlnum |
(DE-627)SPR007862334 (SPR)s00792-013-0615-8-e |
title_full |
Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii |
author_sort |
Prunetti, Laurence |
journal |
Extremophiles |
journalStr |
Extremophiles |
lang_code |
eng |
isOA_bool |
false |
recordtype |
marc |
publishDateSort |
2013 |
contenttype_str_mv |
txt |
container_start_page |
283 |
author_browse |
Prunetti, Laurence Reuter, Christopher J. Hepowit, Nathaniel L. Wu, Yifei Barrueto, Luisa Miranda, Hugo V. Kelly, Karen Maupin-Furlow, Julie A. |
container_volume |
18 |
format_se |
Elektronische Aufsätze |
author-letter |
Prunetti, Laurence |
doi_str_mv |
10.1007/s00792-013-0615-8 |
author2-role |
verfasserin |
title_sort |
structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon haloferax volcanii |
title_auth |
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. |
abstract_unstemmed |
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. |
collection_details |
GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER |
container_issue |
2 |
title_short |
Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii |
url |
https://dx.doi.org/10.1007/s00792-013-0615-8 |
remote_bool |
true |
author2 |
Reuter, Christopher J. Hepowit, Nathaniel L. Wu, Yifei Barrueto, Luisa Miranda, Hugo V. Kelly, Karen Maupin-Furlow, Julie A. |
author2Str |
Reuter, Christopher J. Hepowit, Nathaniel L. Wu, Yifei Barrueto, Luisa Miranda, Hugo V. Kelly, Karen Maupin-Furlow, Julie A. |
ppnlink |
SPR007852657 |
mediatype_str_mv |
c |
isOA_txt |
false |
hochschulschrift_bool |
false |
doi_str |
10.1007/s00792-013-0615-8 |
up_date |
2024-07-03T15:43:42.848Z |
_version_ |
1803573183486361600 |
fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR007862334</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20201124022546.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201005s2013 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s00792-013-0615-8</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR007862334</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s00792-013-0615-8-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Prunetti, Laurence</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Structural and biochemical properties of an extreme ‘salt-loving’ proteasome activating nucleotidase from the archaeon Haloferax volcanii</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2013</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="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.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Archaea</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein modification</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Post-translational modification</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">AAA ATPases</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Proteasomes</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Ubiquitylation</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Sampylation</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Reuter, Christopher J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hepowit, Nathaniel L.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wu, Yifei</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Barrueto, Luisa</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Miranda, Hugo V.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kelly, Karen</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Maupin-Furlow, Julie A.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Extremophiles</subfield><subfield code="d">Springer-Verlag, 2001</subfield><subfield code="g">18(2013), 2 vom: 17. Dez., Seite 283-293</subfield><subfield code="w">(DE-627)SPR007852657</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:18</subfield><subfield code="g">year:2013</subfield><subfield code="g">number:2</subfield><subfield code="g">day:17</subfield><subfield code="g">month:12</subfield><subfield code="g">pages:283-293</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://dx.doi.org/10.1007/s00792-013-0615-8</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_SPRINGER</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">18</subfield><subfield code="j">2013</subfield><subfield code="e">2</subfield><subfield code="b">17</subfield><subfield code="c">12</subfield><subfield code="h">283-293</subfield></datafield></record></collection>
|
score |
7.4011145 |