High-level expression of the angiotensin-converting-enzyme-inhibiting peptide, YG-1, as tandem multimers in Escherichia coli.
Identifieur interne : 003A00 ( Main/Exploration ); précédent : 003999; suivant : 003A01High-level expression of the angiotensin-converting-enzyme-inhibiting peptide, YG-1, as tandem multimers in Escherichia coli.
Auteurs : C J Park [Corée du Sud] ; J H Lee ; S S Hong ; H S Lee ; S C KimSource :
- Applied microbiology and biotechnology [ 0175-7598 ] ; 1998.
Descripteurs français
- KwdFr :
- Analyse de séquence d'ADN, Chromatographie en phase liquide à haute performance, Corps d'inclusion (), Cysteine endopeptidases (), Escherichia coli (), Escherichia coli (métabolisme), Fragments peptidiques (), Fragments peptidiques (isolement et purification), Glyceraldehyde 3-phosphate dehydrogenases (), Inhibiteurs de l'enzyme de conversion de l'angiotensine (), Inhibiteurs de l'enzyme de conversion de l'angiotensine (isolement et purification), Isopropyl-1-thio-bêta-D-galactopyranoside (), Protéines bactériennes (), Régulation de l'expression des gènes bactériens, Saccharomyces cerevisiae (enzymologie), Spectrométrie de masse MALDI, Séquences répétées d'acides nucléiques, Électrophorèse sur gel de polyacrylamide.
- MESH :
- enzymologie : Saccharomyces cerevisiae.
- isolement et purification : Fragments peptidiques, Inhibiteurs de l'enzyme de conversion de l'angiotensine.
- métabolisme : Escherichia coli.
- Analyse de séquence d'ADN, Chromatographie en phase liquide à haute performance, Corps d'inclusion, Cysteine endopeptidases, Escherichia coli, Fragments peptidiques, Glyceraldehyde 3-phosphate dehydrogenases, Inhibiteurs de l'enzyme de conversion de l'angiotensine, Isopropyl-1-thio-bêta-D-galactopyranoside, Protéines bactériennes, Régulation de l'expression des gènes bactériens, Spectrométrie de masse MALDI, Séquences répétées d'acides nucléiques, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Angiotensin-Converting Enzyme Inhibitors (chemistry), Angiotensin-Converting Enzyme Inhibitors (isolation & purification), Bacterial Proteins (chemistry), Chromatography, High Pressure Liquid, Cysteine Endopeptidases (chemistry), Electrophoresis, Polyacrylamide Gel, Escherichia coli (chemistry), Escherichia coli (metabolism), Gene Expression Regulation, Bacterial, Glyceraldehyde-3-Phosphate Dehydrogenases (chemistry), Inclusion Bodies (chemistry), Isopropyl Thiogalactoside (chemistry), Peptide Fragments (chemistry), Peptide Fragments (isolation & purification), Repetitive Sequences, Nucleic Acid, Saccharomyces cerevisiae (enzymology), Sequence Analysis, DNA, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
- MESH :
- chemical , chemistry : Angiotensin-Converting Enzyme Inhibitors, Bacterial Proteins, Cysteine Endopeptidases, Glyceraldehyde-3-Phosphate Dehydrogenases, Isopropyl Thiogalactoside, Peptide Fragments.
- chemical , isolation & purification : Angiotensin-Converting Enzyme Inhibitors, Peptide Fragments.
- chemistry : Escherichia coli, Inclusion Bodies.
- enzymology : Saccharomyces cerevisiae.
- metabolism : Escherichia coli.
- Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Gene Expression Regulation, Bacterial, Repetitive Sequences, Nucleic Acid, Sequence Analysis, DNA, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
Abstract
To produce a large quantity of the angiotensin-converting- enzyme(ACE)-inhibiting peptide YG-1, which consists of ten amino acids derived from yeast glyceraldehyde-3-phosphate dehydrogenase, a high-level expression was explored with tandem multimers of the YG-1 gene in Escherichia coli. The genes encoding YG-1 were tandemly multimerized to 9-mers, 18-mers and 27-mers, in which each of the repeating units in the tandem multimers was connected to the neighboring genes by a DNA linker encoding Pro-Gly-Arg for the cleavage of multimers by clostripain. The multimers were cloned into the expression vector pET-21b, and expressed in E. coli BL21(DE3) with isopropyl beta-D-thiogalactopyranoside induction. The expressed multimeric peptides encoded by the 9-mer, 18-mer and 27-mer accumulated intracellularly as inclusion bodies and comprised about 67%, 25% and 15% of the total proteins in E. coli respectively. The multimeric peptides expressed as inclusion bodies were cleaved with clostripain, and active monomers were purified to homogeneity by reversed-phase high-performance liquid chromatography. In total, 105 mg pure recombinant YG-1 was obtained from 11 E. coli culture harboring pETYG9 which contained the 9-mer of the YG-1 gene. The recombinant YG-1 was identical to the natural YG-1 in molecular mass, amino acid sequence and ACE-inhibiting activity.
DOI: 10.1007/s002530051258
PubMed: 9720202
Affiliations:
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Le document en format XML
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first="H S" last="Lee">H S Lee</name></author><author><name sortKey="Kim, S C" sort="Kim, S C" uniqKey="Kim S" first="S C" last="Kim">S C Kim</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1998">1998</date><idno type="RBID">pubmed:9720202</idno><idno type="pmid">9720202</idno><idno type="doi">10.1007/s002530051258</idno><idno type="wicri:Area/PubMed/Corpus">002672</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002672</idno><idno type="wicri:Area/PubMed/Curation">002672</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002672</idno><idno type="wicri:Area/PubMed/Checkpoint">002533</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002533</idno><idno type="wicri:Area/Ncbi/Merge">002B31</idno><idno type="wicri:Area/Ncbi/Curation">002B31</idno><idno type="wicri:Area/Ncbi/Checkpoint">002B31</idno><idno 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uniqKey="Lee J" first="J H" last="Lee">J H Lee</name></author><author><name sortKey="Hong, S S" sort="Hong, S S" uniqKey="Hong S" first="S S" last="Hong">S S Hong</name></author><author><name sortKey="Lee, H S" sort="Lee, H S" uniqKey="Lee H" first="H S" last="Lee">H S Lee</name></author><author><name sortKey="Kim, S C" sort="Kim, S C" uniqKey="Kim S" first="S C" last="Kim">S C Kim</name></author></analytic><series><title level="j">Applied microbiology and biotechnology</title><idno type="ISSN">0175-7598</idno><imprint><date when="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Angiotensin-Converting Enzyme Inhibitors (chemistry)</term><term>Angiotensin-Converting Enzyme Inhibitors (isolation & purification)</term><term>Bacterial Proteins (chemistry)</term><term>Chromatography, High Pressure Liquid</term><term>Cysteine Endopeptidases (chemistry)</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Escherichia coli (chemistry)</term><term>Escherichia coli (metabolism)</term><term>Gene Expression Regulation, Bacterial</term><term>Glyceraldehyde-3-Phosphate Dehydrogenases (chemistry)</term><term>Inclusion Bodies (chemistry)</term><term>Isopropyl Thiogalactoside (chemistry)</term><term>Peptide Fragments (chemistry)</term><term>Peptide Fragments (isolation & purification)</term><term>Repetitive Sequences, Nucleic Acid</term><term>Saccharomyces cerevisiae (enzymology)</term><term>Sequence Analysis, DNA</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de séquence d'ADN</term><term>Chromatographie en phase liquide à haute performance</term><term>Corps d'inclusion ()</term><term>Cysteine endopeptidases ()</term><term>Escherichia coli ()</term><term>Escherichia coli (métabolisme)</term><term>Fragments peptidiques ()</term><term>Fragments peptidiques (isolement et purification)</term><term>Glyceraldehyde 3-phosphate dehydrogenases ()</term><term>Inhibiteurs de l'enzyme de conversion de l'angiotensine ()</term><term>Inhibiteurs de l'enzyme de conversion de l'angiotensine (isolement et purification)</term><term>Isopropyl-1-thio-bêta-D-galactopyranoside ()</term><term>Protéines bactériennes ()</term><term>Régulation de l'expression des gènes bactériens</term><term>Saccharomyces cerevisiae (enzymologie)</term><term>Spectrométrie de masse MALDI</term><term>Séquences répétées d'acides nucléiques</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Angiotensin-Converting Enzyme Inhibitors</term><term>Bacterial Proteins</term><term>Cysteine Endopeptidases</term><term>Glyceraldehyde-3-Phosphate Dehydrogenases</term><term>Isopropyl Thiogalactoside</term><term>Peptide Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Angiotensin-Converting Enzyme Inhibitors</term><term>Peptide Fragments</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Escherichia coli</term><term>Inclusion Bodies</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Fragments peptidiques</term><term>Inhibiteurs de l'enzyme de conversion de l'angiotensine</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, High Pressure Liquid</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Gene Expression Regulation, Bacterial</term><term>Repetitive Sequences, Nucleic Acid</term><term>Sequence Analysis, DNA</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence d'ADN</term><term>Chromatographie en phase liquide à haute performance</term><term>Corps d'inclusion</term><term>Cysteine endopeptidases</term><term>Escherichia coli</term><term>Fragments peptidiques</term><term>Glyceraldehyde 3-phosphate dehydrogenases</term><term>Inhibiteurs de l'enzyme de conversion de l'angiotensine</term><term>Isopropyl-1-thio-bêta-D-galactopyranoside</term><term>Protéines bactériennes</term><term>Régulation de l'expression des gènes bactériens</term><term>Spectrométrie de masse MALDI</term><term>Séquences répétées d'acides nucléiques</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To produce a large quantity of the angiotensin-converting- enzyme(ACE)-inhibiting peptide YG-1, which consists of ten amino acids derived from yeast glyceraldehyde-3-phosphate dehydrogenase, a high-level expression was explored with tandem multimers of the YG-1 gene in Escherichia coli. The genes encoding YG-1 were tandemly multimerized to 9-mers, 18-mers and 27-mers, in which each of the repeating units in the tandem multimers was connected to the neighboring genes by a DNA linker encoding Pro-Gly-Arg for the cleavage of multimers by clostripain. The multimers were cloned into the expression vector pET-21b, and expressed in E. coli BL21(DE3) with isopropyl beta-D-thiogalactopyranoside induction. The expressed multimeric peptides encoded by the 9-mer, 18-mer and 27-mer accumulated intracellularly as inclusion bodies and comprised about 67%, 25% and 15% of the total proteins in E. coli respectively. The multimeric peptides expressed as inclusion bodies were cleaved with clostripain, and active monomers were purified to homogeneity by reversed-phase high-performance liquid chromatography. In total, 105 mg pure recombinant YG-1 was obtained from 11 E. coli culture harboring pETYG9 which contained the 9-mer of the YG-1 gene. The recombinant YG-1 was identical to the natural YG-1 in molecular mass, amino acid sequence and ACE-inhibiting activity.</div></front></TEI><affiliations><list><country><li>Corée du Sud</li></country></list><tree><noCountry><name sortKey="Hong, S S" sort="Hong, S S" uniqKey="Hong S" first="S S" last="Hong">S S Hong</name><name sortKey="Kim, S C" sort="Kim, S C" uniqKey="Kim S" first="S C" last="Kim">S C Kim</name><name sortKey="Lee, H S" sort="Lee, H S" uniqKey="Lee H" first="H S" last="Lee">H S Lee</name><name sortKey="Lee, J H" sort="Lee, J H" uniqKey="Lee J" first="J H" last="Lee">J H Lee</name></noCountry><country name="Corée du Sud"><noRegion><name sortKey="Park, C J" sort="Park, C J" uniqKey="Park C" first="C J" last="Park">C J Park</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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