Aspen SP1, an exceptional thermal, protease and detergent-resistant self-assembled nano-particle.
Identifieur interne : 003D96 ( Main/Corpus ); précédent : 003D95; suivant : 003D97Aspen SP1, an exceptional thermal, protease and detergent-resistant self-assembled nano-particle.
Auteurs : Wang-Xia Wang ; Or Dgany ; Sharon Grayer Wolf ; Ilan Levy ; Rachel Algom ; Yehonathan Pouny ; Amnon Wolf ; Ira Marton ; Arie Altman ; Oded ShoseyovSource :
- Biotechnology and bioengineering [ 0006-3592 ] ; 2006.
English descriptors
- KwdEn :
- Crystallization (methods), Detergents (chemistry), Dimerization (MeSH), Enzyme Activation (MeSH), Enzyme Stability (MeSH), Multiprotein Complexes (analysis), Multiprotein Complexes (chemistry), Multiprotein Complexes (ultrastructure), Nanostructures (analysis), Nanostructures (chemistry), Nanostructures (ultrastructure), Plant Proteins (analysis), Plant Proteins (chemistry), Plant Proteins (ultrastructure), Populus (enzymology), Protein Binding (MeSH), Temperature (MeSH).
- MESH :
- chemical , analysis : Multiprotein Complexes, Plant Proteins.
- chemical , chemistry : Detergents, Multiprotein Complexes, Plant Proteins.
- analysis : Nanostructures.
- chemistry : Nanostructures.
- enzymology : Populus.
- methods : Crystallization.
- chemical , ultrastructure : Multiprotein Complexes, Nanostructures, Plant Proteins.
- Dimerization, Enzyme Activation, Enzyme Stability, Protein Binding, Temperature.
Abstract
Stable protein 1 (SP1) is a homo-oligomeric protein isolated from aspen (Populus tremula aspen) plants which forms a ring-shape dodecameric particle with a central cavity. The oligomeric form of SP1 is an exceptionally stable structure that is resistant to proteases (e.g., trypsin, V8, and proteinase K), high temperatures, organic solvents, and high levels of ionic detergent. Analytical ultra-centrifugation, chemical cross-linking, matrix-assisted laser-desorption time-of-flight mass spectrometry (MALDI-TOF-MS), and transmission electron microscopy were used to further characterize the SP1 dodecamer. Introduction of a single cysteine at the N-terminus of SP1 enabled the formation of disulfide bridges within the SP1 dodecamer, concurrent with increased melting point. A six-histidine tag was introduced at the N-terminus of SP1 to generate 6HSP1, and the DeltaNSP1 mutant was generated by a deletion of amino acids 2-6 at the N-terminus. Both 6HSP1 and DeltaNSP1 maintained their ability to assemble a stable dodecamer. Remarkably, these SP1 homo-dodecamers were able to re-assemble into stable hetero-dodecamers following co-electro-elution from SDS-PAGE. The exceptional stability of the SP1-nano ring and its ability to self-assemble hetero-complexes paves the way to further research in utilizing this unique protein in nano-biotechnology.
DOI: 10.1002/bit.21010
PubMed: 16732592
Links to Exploration step
pubmed:16732592Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Aspen SP1, an exceptional thermal, protease and detergent-resistant self-assembled nano-particle.</title><author><name sortKey="Wang, Wang Xia" sort="Wang, Wang Xia" uniqKey="Wang W" first="Wang-Xia" last="Wang">Wang-Xia Wang</name><affiliation><nlm:affiliation>The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, and the Otto Warburg Center for Agricultural Biotechnology, Faculty of Agricultural, Food and Environmental Quality Sciences, The Hebrew University of Jerusalem, Israel.</nlm:affiliation></affiliation></author><author><name sortKey="Dgany, Or" sort="Dgany, Or" uniqKey="Dgany O" first="Or" last="Dgany">Or Dgany</name></author><author><name sortKey="Wolf, Sharon Grayer" sort="Wolf, Sharon Grayer" uniqKey="Wolf S" first="Sharon Grayer" last="Wolf">Sharon Grayer Wolf</name></author><author><name sortKey="Levy, Ilan" sort="Levy, Ilan" uniqKey="Levy I" first="Ilan" last="Levy">Ilan Levy</name></author><author><name sortKey="Algom, Rachel" sort="Algom, Rachel" uniqKey="Algom R" first="Rachel" last="Algom">Rachel Algom</name></author><author><name sortKey="Pouny, Yehonathan" sort="Pouny, Yehonathan" uniqKey="Pouny Y" first="Yehonathan" last="Pouny">Yehonathan Pouny</name></author><author><name sortKey="Wolf, Amnon" sort="Wolf, Amnon" uniqKey="Wolf A" first="Amnon" last="Wolf">Amnon Wolf</name></author><author><name sortKey="Marton, Ira" sort="Marton, Ira" uniqKey="Marton I" first="Ira" last="Marton">Ira Marton</name></author><author><name sortKey="Altman, Arie" sort="Altman, Arie" uniqKey="Altman A" first="Arie" last="Altman">Arie Altman</name></author><author><name sortKey="Shoseyov, Oded" sort="Shoseyov, Oded" uniqKey="Shoseyov O" first="Oded" last="Shoseyov">Oded Shoseyov</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16732592</idno><idno type="pmid">16732592</idno><idno type="doi">10.1002/bit.21010</idno><idno type="wicri:Area/Main/Corpus">003D96</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003D96</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Aspen SP1, an exceptional thermal, protease and detergent-resistant self-assembled nano-particle.</title><author><name sortKey="Wang, Wang Xia" sort="Wang, Wang Xia" uniqKey="Wang W" first="Wang-Xia" last="Wang">Wang-Xia Wang</name><affiliation><nlm:affiliation>The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, and the Otto Warburg Center for Agricultural Biotechnology, Faculty of Agricultural, Food and Environmental Quality Sciences, The Hebrew University of Jerusalem, Israel.</nlm:affiliation></affiliation></author><author><name sortKey="Dgany, Or" sort="Dgany, Or" uniqKey="Dgany O" first="Or" last="Dgany">Or Dgany</name></author><author><name sortKey="Wolf, Sharon Grayer" sort="Wolf, Sharon Grayer" uniqKey="Wolf S" first="Sharon Grayer" last="Wolf">Sharon Grayer Wolf</name></author><author><name sortKey="Levy, Ilan" sort="Levy, Ilan" uniqKey="Levy I" first="Ilan" last="Levy">Ilan Levy</name></author><author><name sortKey="Algom, Rachel" sort="Algom, Rachel" uniqKey="Algom R" first="Rachel" last="Algom">Rachel Algom</name></author><author><name sortKey="Pouny, Yehonathan" sort="Pouny, Yehonathan" uniqKey="Pouny Y" first="Yehonathan" last="Pouny">Yehonathan Pouny</name></author><author><name sortKey="Wolf, Amnon" sort="Wolf, Amnon" uniqKey="Wolf A" first="Amnon" last="Wolf">Amnon Wolf</name></author><author><name sortKey="Marton, Ira" sort="Marton, Ira" uniqKey="Marton I" first="Ira" last="Marton">Ira Marton</name></author><author><name sortKey="Altman, Arie" sort="Altman, Arie" uniqKey="Altman A" first="Arie" last="Altman">Arie Altman</name></author><author><name sortKey="Shoseyov, Oded" sort="Shoseyov, Oded" uniqKey="Shoseyov O" first="Oded" last="Shoseyov">Oded Shoseyov</name></author></analytic><series><title level="j">Biotechnology and bioengineering</title><idno type="ISSN">0006-3592</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Crystallization (methods)</term><term>Detergents (chemistry)</term><term>Dimerization (MeSH)</term><term>Enzyme Activation (MeSH)</term><term>Enzyme Stability (MeSH)</term><term>Multiprotein Complexes (analysis)</term><term>Multiprotein Complexes (chemistry)</term><term>Multiprotein Complexes (ultrastructure)</term><term>Nanostructures (analysis)</term><term>Nanostructures (chemistry)</term><term>Nanostructures (ultrastructure)</term><term>Plant Proteins (analysis)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (ultrastructure)</term><term>Populus (enzymology)</term><term>Protein Binding (MeSH)</term><term>Temperature (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Multiprotein Complexes</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Detergents</term><term>Multiprotein Complexes</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="analysis" xml:lang="en"><term>Nanostructures</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanostructures</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Crystallization</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Multiprotein Complexes</term><term>Nanostructures</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Dimerization</term><term>Enzyme Activation</term><term>Enzyme Stability</term><term>Protein Binding</term><term>Temperature</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Stable protein 1 (SP1) is a homo-oligomeric protein isolated from aspen (Populus tremula aspen) plants which forms a ring-shape dodecameric particle with a central cavity. The oligomeric form of SP1 is an exceptionally stable structure that is resistant to proteases (e.g., trypsin, V8, and proteinase K), high temperatures, organic solvents, and high levels of ionic detergent. Analytical ultra-centrifugation, chemical cross-linking, matrix-assisted laser-desorption time-of-flight mass spectrometry (MALDI-TOF-MS), and transmission electron microscopy were used to further characterize the SP1 dodecamer. Introduction of a single cysteine at the N-terminus of SP1 enabled the formation of disulfide bridges within the SP1 dodecamer, concurrent with increased melting point. A six-histidine tag was introduced at the N-terminus of SP1 to generate 6HSP1, and the DeltaNSP1 mutant was generated by a deletion of amino acids 2-6 at the N-terminus. Both 6HSP1 and DeltaNSP1 maintained their ability to assemble a stable dodecamer. Remarkably, these SP1 homo-dodecamers were able to re-assemble into stable hetero-dodecamers following co-electro-elution from SDS-PAGE. The exceptional stability of the SP1-nano ring and its ability to self-assemble hetero-complexes paves the way to further research in utilizing this unique protein in nano-biotechnology.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16732592</PMID><DateCompleted><Year>2006</Year><Month>10</Month><Day>05</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3592</ISSN><JournalIssue CitedMedium="Print"><Volume>95</Volume><Issue>1</Issue><PubDate><Year>2006</Year><Month>Sep</Month><Day>05</Day></PubDate></JournalIssue><Title>Biotechnology and bioengineering</Title><ISOAbbreviation>Biotechnol Bioeng</ISOAbbreviation></Journal><ArticleTitle>Aspen SP1, an exceptional thermal, protease and detergent-resistant self-assembled nano-particle.</ArticleTitle><Pagination><MedlinePgn>161-8</MedlinePgn></Pagination><Abstract><AbstractText>Stable protein 1 (SP1) is a homo-oligomeric protein isolated from aspen (Populus tremula aspen) plants which forms a ring-shape dodecameric particle with a central cavity. The oligomeric form of SP1 is an exceptionally stable structure that is resistant to proteases (e.g., trypsin, V8, and proteinase K), high temperatures, organic solvents, and high levels of ionic detergent. Analytical ultra-centrifugation, chemical cross-linking, matrix-assisted laser-desorption time-of-flight mass spectrometry (MALDI-TOF-MS), and transmission electron microscopy were used to further characterize the SP1 dodecamer. Introduction of a single cysteine at the N-terminus of SP1 enabled the formation of disulfide bridges within the SP1 dodecamer, concurrent with increased melting point. A six-histidine tag was introduced at the N-terminus of SP1 to generate 6HSP1, and the DeltaNSP1 mutant was generated by a deletion of amino acids 2-6 at the N-terminus. Both 6HSP1 and DeltaNSP1 maintained their ability to assemble a stable dodecamer. Remarkably, these SP1 homo-dodecamers were able to re-assemble into stable hetero-dodecamers following co-electro-elution from SDS-PAGE. The exceptional stability of the SP1-nano ring and its ability to self-assemble hetero-complexes paves the way to further research in utilizing this unique protein in nano-biotechnology.</AbstractText><CopyrightInformation>(c) 2006 Wiley Periodicals, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Wang-Xia</ForeName><Initials>WX</Initials><AffiliationInfo><Affiliation>The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, and the Otto Warburg Center for Agricultural Biotechnology, Faculty of Agricultural, Food and Environmental Quality Sciences, The Hebrew University of Jerusalem, Israel.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dgany</LastName><ForeName>Or</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Wolf</LastName><ForeName>Sharon Grayer</ForeName><Initials>SG</Initials></Author><Author ValidYN="Y"><LastName>Levy</LastName><ForeName>Ilan</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Algom</LastName><ForeName>Rachel</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Pouny</LastName><ForeName>Yehonathan</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Wolf</LastName><ForeName>Amnon</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Marton</LastName><ForeName>Ira</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Altman</LastName><ForeName>Arie</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Shoseyov</LastName><ForeName>Oded</ForeName><Initials>O</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biotechnol Bioeng</MedlineTA><NlmUniqueID>7502021</NlmUniqueID><ISSNLinking>0006-3592</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003902">Detergents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003902" MajorTopicYN="N">Detergents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D049329" MajorTopicYN="N">Nanostructures</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>5</Month><Day>30</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>10</Month><Day>6</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>5</Month><Day>30</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16732592</ArticleId><ArticleId IdType="doi">10.1002/bit.21010</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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