Specific and efficient cleavage of fusion proteins by recombinant plum pox virus NIa protease.
Identifieur interne : 001C77 ( PubMed/Corpus ); précédent : 001C76; suivant : 001C78Specific and efficient cleavage of fusion proteins by recombinant plum pox virus NIa protease.
Auteurs : Nuoyan Zheng ; José De Jesús Pérez ; Zhonghui Zhang ; Elvira Domínguez ; Juan Antonio Garcia ; Qi XieSource :
- Protein expression and purification [ 1046-5928 ] ; 2008.
English descriptors
- KwdEn :
- Amino Acid Sequence, Capsid Proteins (isolation & purification), Capsid Proteins (metabolism), Endopeptidases (chemistry), Endopeptidases (isolation & purification), Endopeptidases (metabolism), Enzyme Stability (drug effects), Escherichia coli (metabolism), Green Fluorescent Proteins (isolation & purification), Green Fluorescent Proteins (metabolism), Molecular Sequence Data, Osmolar Concentration, Plum Pox Virus (enzymology), Protease Inhibitors (pharmacology), Protein Processing, Post-Translational (drug effects), Recombinant Fusion Proteins (isolation & purification), Recombinant Fusion Proteins (metabolism), Sequence Alignment, Sodium Chloride (pharmacology), Substrate Specificity (drug effects), Temperature, Viral Proteins (chemistry), Viral Proteins (isolation & purification), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Endopeptidases, Viral Proteins.
- chemical , isolation & purification : Capsid Proteins, Endopeptidases, Green Fluorescent Proteins, Recombinant Fusion Proteins, Viral Proteins.
- chemical , metabolism : Capsid Proteins, Endopeptidases, Green Fluorescent Proteins, Recombinant Fusion Proteins, Viral Proteins.
- drug effects : Enzyme Stability, Protein Processing, Post-Translational, Substrate Specificity.
- enzymology : Plum Pox Virus.
- metabolism : Escherichia coli.
- chemical , pharmacology : Protease Inhibitors, Sodium Chloride.
- Amino Acid Sequence, Molecular Sequence Data, Osmolar Concentration, Sequence Alignment, Temperature.
Abstract
Site-specific proteases are the most popular kind of enzymes for removing the fusion tags from fused target proteins. Nuclear inclusion protein a (NIa) proteases obtained from the family Potyviridae have become promising due to their high activities and stringencies of sequences recognition. NIa proteases from tobacco etch virus (TEV) and tomato vein mottling virus (TVMV) have been shown to process recombinant proteins successfully in vitro. In this report, recombinant PPV (plum pox virus) NIa protease was employed to process fusion proteins with artificial cleavage site in vitro. Characteristics such as catalytic ability and affecting factors (salt, temperature, protease inhibitors, detergents, and denaturing reagents) were investigated. Recombinant PPV NIa protease expressed and purified from Escherichia coli demonstrated efficient and specific processing of recombinant GFP and SARS-CoV nucleocapsid protein, with site F (N V V V H Q black triangle down A) for PPV NIa protease artificially inserted between the fusion tags and the target proteins. Its catalytic capability is similar to those of TVMV and TEV NIa protease. Recombinant PPV NIa protease reached its maximal proteolytic activity at approximately 30 degrees C. Salt concentration and only one of the tested protease inhibitors had minor influences on the proteolytic activity of PPV NIa protease. Recombinant PPV NIa protease was resistant to self-lysis for at least five days.
DOI: 10.1016/j.pep.2007.10.008
PubMed: 18024078
Links to Exploration step
pubmed:18024078Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Specific and efficient cleavage of fusion proteins by recombinant plum pox virus NIa protease.</title><author><name sortKey="Zheng, Nuoyan" sort="Zheng, Nuoyan" uniqKey="Zheng N" first="Nuoyan" last="Zheng">Nuoyan Zheng</name><affiliation><nlm:affiliation>State Key Laboratory for Biocontrol, Sun Yat-sen (Zhongshan) University, 135 Xinggang Road W, Guangzhou 510275, China.</nlm:affiliation></affiliation></author><author><name sortKey="Perez, Jose De Jesus" sort="Perez, Jose De Jesus" uniqKey="Perez J" first="José De Jesús" last="Pérez">José De Jesús Pérez</name></author><author><name sortKey="Zhang, Zhonghui" sort="Zhang, Zhonghui" uniqKey="Zhang Z" first="Zhonghui" last="Zhang">Zhonghui Zhang</name></author><author><name sortKey="Dominguez, Elvira" sort="Dominguez, Elvira" uniqKey="Dominguez E" first="Elvira" last="Domínguez">Elvira Domínguez</name></author><author><name sortKey="Garcia, Juan Antonio" sort="Garcia, Juan Antonio" uniqKey="Garcia J" first="Juan Antonio" last="Garcia">Juan Antonio Garcia</name></author><author><name sortKey="Xie, Qi" sort="Xie, Qi" uniqKey="Xie Q" first="Qi" last="Xie">Qi Xie</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18024078</idno><idno type="pmid">18024078</idno><idno type="doi">10.1016/j.pep.2007.10.008</idno><idno type="wicri:Area/PubMed/Corpus">001C77</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001C77</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Specific and efficient cleavage of fusion proteins by recombinant plum pox virus NIa protease.</title><author><name sortKey="Zheng, Nuoyan" sort="Zheng, Nuoyan" uniqKey="Zheng N" first="Nuoyan" last="Zheng">Nuoyan Zheng</name><affiliation><nlm:affiliation>State Key Laboratory for Biocontrol, Sun Yat-sen (Zhongshan) University, 135 Xinggang Road W, Guangzhou 510275, China.</nlm:affiliation></affiliation></author><author><name sortKey="Perez, Jose De Jesus" sort="Perez, Jose De Jesus" uniqKey="Perez J" first="José De Jesús" last="Pérez">José De Jesús Pérez</name></author><author><name sortKey="Zhang, Zhonghui" sort="Zhang, Zhonghui" uniqKey="Zhang Z" first="Zhonghui" last="Zhang">Zhonghui Zhang</name></author><author><name sortKey="Dominguez, Elvira" sort="Dominguez, Elvira" uniqKey="Dominguez E" first="Elvira" last="Domínguez">Elvira Domínguez</name></author><author><name sortKey="Garcia, Juan Antonio" sort="Garcia, Juan Antonio" uniqKey="Garcia J" first="Juan Antonio" last="Garcia">Juan Antonio Garcia</name></author><author><name sortKey="Xie, Qi" sort="Xie, Qi" uniqKey="Xie Q" first="Qi" last="Xie">Qi Xie</name></author></analytic><series><title level="j">Protein expression and purification</title><idno type="ISSN">1046-5928</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Capsid Proteins (isolation & purification)</term><term>Capsid Proteins (metabolism)</term><term>Endopeptidases (chemistry)</term><term>Endopeptidases (isolation & purification)</term><term>Endopeptidases (metabolism)</term><term>Enzyme Stability (drug effects)</term><term>Escherichia coli (metabolism)</term><term>Green Fluorescent Proteins (isolation & purification)</term><term>Green Fluorescent Proteins (metabolism)</term><term>Molecular Sequence Data</term><term>Osmolar Concentration</term><term>Plum Pox Virus (enzymology)</term><term>Protease Inhibitors (pharmacology)</term><term>Protein Processing, Post-Translational (drug effects)</term><term>Recombinant Fusion Proteins (isolation & purification)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Sequence Alignment</term><term>Sodium Chloride (pharmacology)</term><term>Substrate Specificity (drug effects)</term><term>Temperature</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (isolation & purification)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Endopeptidases</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Capsid Proteins</term><term>Endopeptidases</term><term>Green Fluorescent Proteins</term><term>Recombinant Fusion Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Capsid Proteins</term><term>Endopeptidases</term><term>Green Fluorescent Proteins</term><term>Recombinant Fusion Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Enzyme Stability</term><term>Protein Processing, Post-Translational</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plum Pox Virus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Protease Inhibitors</term><term>Sodium Chloride</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Molecular Sequence Data</term><term>Osmolar Concentration</term><term>Sequence Alignment</term><term>Temperature</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Site-specific proteases are the most popular kind of enzymes for removing the fusion tags from fused target proteins. Nuclear inclusion protein a (NIa) proteases obtained from the family Potyviridae have become promising due to their high activities and stringencies of sequences recognition. NIa proteases from tobacco etch virus (TEV) and tomato vein mottling virus (TVMV) have been shown to process recombinant proteins successfully in vitro. In this report, recombinant PPV (plum pox virus) NIa protease was employed to process fusion proteins with artificial cleavage site in vitro. Characteristics such as catalytic ability and affecting factors (salt, temperature, protease inhibitors, detergents, and denaturing reagents) were investigated. Recombinant PPV NIa protease expressed and purified from Escherichia coli demonstrated efficient and specific processing of recombinant GFP and SARS-CoV nucleocapsid protein, with site F (N V V V H Q black triangle down A) for PPV NIa protease artificially inserted between the fusion tags and the target proteins. Its catalytic capability is similar to those of TVMV and TEV NIa protease. Recombinant PPV NIa protease reached its maximal proteolytic activity at approximately 30 degrees C. Salt concentration and only one of the tested protease inhibitors had minor influences on the proteolytic activity of PPV NIa protease. Recombinant PPV NIa protease was resistant to self-lysis for at least five days.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18024078</PMID><DateCompleted><Year>2008</Year><Month>03</Month><Day>13</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1046-5928</ISSN><JournalIssue CitedMedium="Print"><Volume>57</Volume><Issue>2</Issue><PubDate><Year>2008</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Protein expression and purification</Title><ISOAbbreviation>Protein Expr. Purif.</ISOAbbreviation></Journal><ArticleTitle>Specific and efficient cleavage of fusion proteins by recombinant plum pox virus NIa protease.</ArticleTitle><Pagination><MedlinePgn>153-62</MedlinePgn></Pagination><Abstract><AbstractText>Site-specific proteases are the most popular kind of enzymes for removing the fusion tags from fused target proteins. Nuclear inclusion protein a (NIa) proteases obtained from the family Potyviridae have become promising due to their high activities and stringencies of sequences recognition. NIa proteases from tobacco etch virus (TEV) and tomato vein mottling virus (TVMV) have been shown to process recombinant proteins successfully in vitro. In this report, recombinant PPV (plum pox virus) NIa protease was employed to process fusion proteins with artificial cleavage site in vitro. Characteristics such as catalytic ability and affecting factors (salt, temperature, protease inhibitors, detergents, and denaturing reagents) were investigated. Recombinant PPV NIa protease expressed and purified from Escherichia coli demonstrated efficient and specific processing of recombinant GFP and SARS-CoV nucleocapsid protein, with site F (N V V V H Q black triangle down A) for PPV NIa protease artificially inserted between the fusion tags and the target proteins. Its catalytic capability is similar to those of TVMV and TEV NIa protease. Recombinant PPV NIa protease reached its maximal proteolytic activity at approximately 30 degrees C. Salt concentration and only one of the tested protease inhibitors had minor influences on the proteolytic activity of PPV NIa protease. Recombinant PPV NIa protease was resistant to self-lysis for at least five days.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zheng</LastName><ForeName>Nuoyan</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>State Key Laboratory for Biocontrol, Sun Yat-sen (Zhongshan) University, 135 Xinggang Road W, Guangzhou 510275, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pérez</LastName><ForeName>José de Jesús</ForeName><Initials>Jde J</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Zhonghui</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Domínguez</LastName><ForeName>Elvira</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Garcia</LastName><ForeName>Juan Antonio</ForeName><Initials>JA</Initials></Author><Author 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purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2007</Year><Month>08</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2007</Year><Month>09</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>10</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>11</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>3</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>11</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18024078</ArticleId><ArticleId 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