Molecular cloning, sequencing, expression of Chinese sturgeon cystatin in yeast Pichia pastoris and its proteinase inhibitory activity.
Identifieur interne : 000485 ( PubMed/Checkpoint ); précédent : 000484; suivant : 000486Molecular cloning, sequencing, expression of Chinese sturgeon cystatin in yeast Pichia pastoris and its proteinase inhibitory activity.
Auteurs : Junjie Bai [République populaire de Chine] ; Dongmei Ma ; Haihua Lao ; Qing Jian ; Xing Ye ; Jianren Luo ; Xiaoyong Xong ; Yinghua Li ; Xufang LiangSource :
- Journal of biotechnology [ 0168-1656 ] ; 2006.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Base Sequence, Cathepsin B (antagonists & inhibitors), Cathepsin B (metabolism), Cloning, Molecular, Cystatins (genetics), Cystatins (metabolism), Cystatins (pharmacology), DNA, Complementary (chemistry), DNA, Complementary (genetics), Electrophoresis, Polyacrylamide Gel, Enzyme Stability, Fish Proteins (genetics), Fish Proteins (metabolism), Fish Proteins (pharmacology), Fishes (genetics), Fishes (metabolism), Gene Expression (genetics), Hot Temperature, Hydrogen-Ion Concentration, Molecular Sequence Data, Papain (antagonists & inhibitors), Papain (metabolism), Pichia (genetics), Protease Inhibitors (pharmacology), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Recombinant Proteins (pharmacology), Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Amino Acid.
- MESH :
- chemical , antagonists & inhibitors : Cathepsin B, Papain.
- chemical , chemistry : DNA, Complementary.
- chemical , genetics : Cystatins, DNA, Complementary, Fish Proteins.
- chemical , isolation & purification : Recombinant Proteins.
- chemical , metabolism : Cathepsin B, Cystatins, Fish Proteins, Papain, Recombinant Proteins.
- chemical , pharmacology : Cystatins, Fish Proteins, Protease Inhibitors, Recombinant Proteins.
- genetics : Fishes, Gene Expression, Pichia.
- metabolism : Fishes.
- Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Enzyme Stability, Hot Temperature, Hydrogen-Ion Concentration, Molecular Sequence Data, Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Amino Acid.
Abstract
Cystatin, a superfamily of cysteine proteinase inhibitor of cathepsins and other cysteine proteinases, is widely distributed in animal tissues and body fluids. Although considerable attention has been given to mammalian and avian cystatins, little is known about cystatins from other vertebrates. In this study, a cDNA coding for Chinese sturgeon (Acipenser sinensis) cystatin was isolated and characterized. The corresponding mature cystatin peptide cDNA is 336 nucleotides long and encodes a protein of 112 amino acids. Sequence comparison showed that the cloned cystatin was a homolog of the mammalian Family II cystatin. The cystatin cDNA of Chinese sturgeon was subcloned into yeast expression vector pPICZalphaA and transformed into Pichia pastoris GS115 strain. After methanol induction, SDS-PAGE analysis of the culture supernatant indicated that the yield of recombinant cystatin was about 215 mg/l medium supernatant in shaking-flask fermentation medium, accounting for 73.6% of the total supernatant secreted proteins. Our data also showed that the recombinant cystatin is active in inhibiting the protease activity of papain and cathepsin B. Heat stability of the recombinant cystatin was also measured.
DOI: 10.1016/j.jbiotec.2006.02.023
PubMed: 16713004
Affiliations:
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first="Dongmei" last="Ma">Dongmei Ma</name></author><author><name sortKey="Lao, Haihua" sort="Lao, Haihua" uniqKey="Lao H" first="Haihua" last="Lao">Haihua Lao</name></author><author><name sortKey="Jian, Qing" sort="Jian, Qing" uniqKey="Jian Q" first="Qing" last="Jian">Qing Jian</name></author><author><name sortKey="Ye, Xing" sort="Ye, Xing" uniqKey="Ye X" first="Xing" last="Ye">Xing Ye</name></author><author><name sortKey="Luo, Jianren" sort="Luo, Jianren" uniqKey="Luo J" first="Jianren" last="Luo">Jianren Luo</name></author><author><name sortKey="Xong, Xiaoyong" sort="Xong, Xiaoyong" uniqKey="Xong X" first="Xiaoyong" last="Xong">Xiaoyong Xong</name></author><author><name sortKey="Li, Yinghua" sort="Li, Yinghua" uniqKey="Li Y" first="Yinghua" last="Li">Yinghua Li</name></author><author><name sortKey="Liang, Xufang" sort="Liang, Xufang" uniqKey="Liang X" first="Xufang" last="Liang">Xufang Liang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date 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Institute, CAFS Key Laboratory of Tropical & Subtropical Fish Breeding & Cultivation of CAFS, Guangzhou 510380, PR China. jjbai@163.net</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Pearl River Fisheries Research Institute, CAFS Key Laboratory of Tropical & Subtropical Fish Breeding & Cultivation of CAFS, Guangzhou 510380</wicri:regionArea><placeName><settlement type="city">Jiangmen</settlement><region type="province">Guangdong</region></placeName></affiliation></author><author><name sortKey="Ma, Dongmei" sort="Ma, Dongmei" uniqKey="Ma D" first="Dongmei" last="Ma">Dongmei Ma</name></author><author><name sortKey="Lao, Haihua" sort="Lao, Haihua" uniqKey="Lao H" first="Haihua" last="Lao">Haihua Lao</name></author><author><name sortKey="Jian, Qing" sort="Jian, Qing" uniqKey="Jian Q" first="Qing" last="Jian">Qing Jian</name></author><author><name sortKey="Ye, Xing" sort="Ye, Xing" uniqKey="Ye X" first="Xing" last="Ye">Xing Ye</name></author><author><name sortKey="Luo, Jianren" sort="Luo, Jianren" uniqKey="Luo J" first="Jianren" last="Luo">Jianren Luo</name></author><author><name sortKey="Xong, Xiaoyong" sort="Xong, Xiaoyong" uniqKey="Xong X" first="Xiaoyong" last="Xong">Xiaoyong Xong</name></author><author><name sortKey="Li, Yinghua" sort="Li, Yinghua" uniqKey="Li Y" first="Yinghua" last="Li">Yinghua Li</name></author><author><name sortKey="Liang, Xufang" sort="Liang, Xufang" uniqKey="Liang X" first="Xufang" last="Liang">Xufang Liang</name></author></analytic><series><title level="j">Journal of biotechnology</title><idno type="ISSN">0168-1656</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cathepsin B (antagonists & inhibitors)</term><term>Cathepsin B (metabolism)</term><term>Cloning, Molecular</term><term>Cystatins (genetics)</term><term>Cystatins (metabolism)</term><term>Cystatins (pharmacology)</term><term>DNA, Complementary (chemistry)</term><term>DNA, Complementary (genetics)</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Enzyme Stability</term><term>Fish Proteins (genetics)</term><term>Fish Proteins (metabolism)</term><term>Fish Proteins (pharmacology)</term><term>Fishes (genetics)</term><term>Fishes (metabolism)</term><term>Gene Expression (genetics)</term><term>Hot Temperature</term><term>Hydrogen-Ion Concentration</term><term>Molecular Sequence Data</term><term>Papain (antagonists & inhibitors)</term><term>Papain (metabolism)</term><term>Pichia (genetics)</term><term>Protease Inhibitors (pharmacology)</term><term>Recombinant Proteins (isolation & purification)</term><term>Recombinant Proteins (metabolism)</term><term>Recombinant Proteins (pharmacology)</term><term>Sequence Alignment</term><term>Sequence Analysis, DNA</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Cathepsin B</term><term>Papain</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA, Complementary</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cystatins</term><term>DNA, Complementary</term><term>Fish Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cathepsin B</term><term>Cystatins</term><term>Fish Proteins</term><term>Papain</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cystatins</term><term>Fish Proteins</term><term>Protease Inhibitors</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Fishes</term><term>Gene Expression</term><term>Pichia</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Enzyme Stability</term><term>Hot Temperature</term><term>Hydrogen-Ion Concentration</term><term>Molecular Sequence Data</term><term>Sequence Alignment</term><term>Sequence Analysis, DNA</term><term>Sequence Homology, Amino Acid</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cystatin, a superfamily of cysteine proteinase inhibitor of cathepsins and other cysteine proteinases, is widely distributed in animal tissues and body fluids. Although considerable attention has been given to mammalian and avian cystatins, little is known about cystatins from other vertebrates. In this study, a cDNA coding for Chinese sturgeon (Acipenser sinensis) cystatin was isolated and characterized. The corresponding mature cystatin peptide cDNA is 336 nucleotides long and encodes a protein of 112 amino acids. Sequence comparison showed that the cloned cystatin was a homolog of the mammalian Family II cystatin. The cystatin cDNA of Chinese sturgeon was subcloned into yeast expression vector pPICZalphaA and transformed into Pichia pastoris GS115 strain. After methanol induction, SDS-PAGE analysis of the culture supernatant indicated that the yield of recombinant cystatin was about 215 mg/l medium supernatant in shaking-flask fermentation medium, accounting for 73.6% of the total supernatant secreted proteins. Our data also showed that the recombinant cystatin is active in inhibiting the protease activity of papain and cathepsin B. Heat stability of the recombinant cystatin was also measured.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16713004</PMID><DateCreated><Year>2006</Year><Month>08</Month><Day>14</Day></DateCreated><DateCompleted><Year>2006</Year><Month>10</Month><Day>03</Day></DateCompleted><DateRevised><Year>2008</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0168-1656</ISSN><JournalIssue CitedMedium="Print"><Volume>125</Volume><Issue>2</Issue><PubDate><Year>2006</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of biotechnology</Title><ISOAbbreviation>J. Biotechnol.</ISOAbbreviation></Journal><ArticleTitle>Molecular cloning, sequencing, expression of Chinese sturgeon cystatin in yeast Pichia pastoris and its proteinase inhibitory activity.</ArticleTitle><Pagination><MedlinePgn>231-41</MedlinePgn></Pagination><Abstract><AbstractText>Cystatin, a superfamily of cysteine proteinase inhibitor of cathepsins and other cysteine proteinases, is widely distributed in animal tissues and body fluids. Although considerable attention has been given to mammalian and avian cystatins, little is known about cystatins from other vertebrates. In this study, a cDNA coding for Chinese sturgeon (Acipenser sinensis) cystatin was isolated and characterized. The corresponding mature cystatin peptide cDNA is 336 nucleotides long and encodes a protein of 112 amino acids. Sequence comparison showed that the cloned cystatin was a homolog of the mammalian Family II cystatin. The cystatin cDNA of Chinese sturgeon was subcloned into yeast expression vector pPICZalphaA and transformed into Pichia pastoris GS115 strain. After methanol induction, SDS-PAGE analysis of the culture supernatant indicated that the yield of recombinant cystatin was about 215 mg/l medium supernatant in shaking-flask fermentation medium, accounting for 73.6% of the total supernatant secreted proteins. Our data also showed that the recombinant cystatin is active in inhibiting the protease activity of papain and cathepsin B. Heat stability of the recombinant cystatin was also measured.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bai</LastName><ForeName>Junjie</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Pearl River Fisheries Research Institute, CAFS Key Laboratory of Tropical & Subtropical Fish Breeding & Cultivation of CAFS, Guangzhou 510380, PR China. jjbai@163.net</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ma</LastName><ForeName>Dongmei</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Lao</LastName><ForeName>Haihua</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Jian</LastName><ForeName>Qing</ForeName><Initials>Q</Initials></Author><Author ValidYN="Y"><LastName>Ye</LastName><ForeName>Xing</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Luo</LastName><ForeName>Jianren</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Xong</LastName><ForeName>Xiaoyong</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Yinghua</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Liang</LastName><ForeName>Xufang</ForeName><Initials>X</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AF334611</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>05</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Biotechnol</MedlineTA><NlmUniqueID>8411927</NlmUniqueID><ISSNLinking>0168-1656</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015891">Cystatins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029941">Fish Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.1</RegistryNumber><NameOfSubstance UI="D002401">Cathepsin B</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.2</RegistryNumber><NameOfSubstance UI="D010206">Papain</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002401" MajorTopicYN="N">Cathepsin B</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015891" MajorTopicYN="N">Cystatins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D029941" MajorTopicYN="N">Fish Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005399" MajorTopicYN="N">Fishes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="N">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010206" MajorTopicYN="N">Papain</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010843" MajorTopicYN="N">Pichia</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017422" MajorTopicYN="N">Sequence Analysis, DNA</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2005</Year><Month>08</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2006</Year><Month>01</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>02</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>5</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>10</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>5</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16713004</ArticleId><ArticleId IdType="pii">S0168-1656(06)00164-7</ArticleId><ArticleId IdType="doi">10.1016/j.jbiotec.2006.02.023</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country><region><li>Guangdong</li></region><settlement><li>Jiangmen</li></settlement></list><tree><noCountry><name sortKey="Jian, Qing" sort="Jian, Qing" uniqKey="Jian Q" first="Qing" last="Jian">Qing Jian</name><name sortKey="Lao, Haihua" sort="Lao, Haihua" uniqKey="Lao H" first="Haihua" last="Lao">Haihua Lao</name><name sortKey="Li, Yinghua" sort="Li, Yinghua" uniqKey="Li Y" first="Yinghua" last="Li">Yinghua Li</name><name sortKey="Liang, Xufang" sort="Liang, Xufang" uniqKey="Liang X" first="Xufang" last="Liang">Xufang Liang</name><name sortKey="Luo, Jianren" sort="Luo, Jianren" uniqKey="Luo J" first="Jianren" last="Luo">Jianren Luo</name><name sortKey="Ma, Dongmei" sort="Ma, Dongmei" uniqKey="Ma D" first="Dongmei" last="Ma">Dongmei Ma</name><name sortKey="Xong, Xiaoyong" sort="Xong, Xiaoyong" uniqKey="Xong X" first="Xiaoyong" last="Xong">Xiaoyong Xong</name><name sortKey="Ye, Xing" sort="Ye, Xing" uniqKey="Ye X" first="Xing" last="Ye">Xing Ye</name></noCountry><country name="République populaire de Chine"><region name="Guangdong"><name sortKey="Bai, Junjie" sort="Bai, Junjie" uniqKey="Bai J" first="Junjie" last="Bai">Junjie Bai</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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