Exploring sequence-function space of a poplar glutathione transferase using designed information-rich gene variants.
Identifieur interne : 001395 ( Main/Exploration ); précédent : 001394; suivant : 001396Exploring sequence-function space of a poplar glutathione transferase using designed information-rich gene variants.
Auteurs : Yaman Musdal [Suède] ; Sridhar Govindarajan [États-Unis] ; Bengt Mannervik [Suède]Source :
- Protein engineering, design & selection : PEDS [ 1741-0134 ] ; 2017.
Descripteurs français
- KwdFr :
- Escherichia coli (génétique), Glutathione transferase (composition chimique), Glutathione transferase (génétique), Glutathione transferase (métabolisme), Ingénierie des protéines (MeSH), Modèles moléculaires (MeSH), Populus (enzymologie), Populus (génétique), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines végétales (composition chimique), Protéines végétales (génétique), Protéines végétales (métabolisme), Évolution moléculaire dirigée (méthodes).
- MESH :
- composition chimique : Glutathione transferase, Protéines recombinantes, Protéines végétales.
- enzymologie : Populus.
- génétique : Escherichia coli, Glutathione transferase, Populus, Protéines recombinantes, Protéines végétales.
- métabolisme : Glutathione transferase, Protéines recombinantes, Protéines végétales.
- méthodes : Évolution moléculaire dirigée.
- Ingénierie des protéines, Modèles moléculaires.
English descriptors
- KwdEn :
- Directed Molecular Evolution (methods), Escherichia coli (genetics), Glutathione Transferase (chemistry), Glutathione Transferase (genetics), Glutathione Transferase (metabolism), Models, Molecular (MeSH), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (metabolism), Populus (enzymology), Populus (genetics), Protein Engineering (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism).
- MESH :
- chemical , chemistry : Glutathione Transferase, Plant Proteins, Recombinant Proteins.
- enzymology : Populus.
- genetics : Escherichia coli, Glutathione Transferase, Plant Proteins, Populus, Recombinant Proteins.
- chemical , metabolism : Glutathione Transferase, Plant Proteins, Recombinant Proteins.
- methods : Directed Molecular Evolution.
- Models, Molecular, Protein Engineering.
Abstract
Exploring the vicinity around a locus of a protein in sequence space may identify homologs with enhanced properties, which could become valuable in biotechnical and other applications. A rational approach to this pursuit is the use of 'infologs', i.e. synthetic sequences with specific substitutions capturing maximal sequence information derived from the evolutionary history of the protein family. Ninety-five such infolog genes of poplar glutathione transferase were synthesized and expressed in Escherichia coli, and the catalytic activities of the proteins determined with alternative substrates. Sequence-activity relationships derived from the infologs were used to design a second set of 47 infologs in which 90% of the members exceeded wild-type properties. Two mutants, C2 (V55I/E95D/D108E/A160V) and G5 (F13L/C70A/G122E), were further functionally characterized. The activities of the infologs with the alternative substrates 1-chloro-2,4-dinitrobenzene and phenethyl isothiocyanate, subject to different chemistries, were positively correlated, indicating that the examined mutations were affecting the overall catalytic competence without major shift in substrate discrimination. By contrast, the enhanced protein expressivity observed in many of the mutants were not similarly correlated with the activities. In conclusion, small libraries of well-defined infologs can be used to systematically explore sequence space to optimize proteins in multidimensional functional space.
DOI: 10.1093/protein/gzx045
PubMed: 28967959
PubMed Central: PMC5914380
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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xml:lang="en"><term>Directed Molecular Evolution</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathione transferase</term><term>Protéines recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Évolution moléculaire dirigée</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Models, Molecular</term><term>Protein Engineering</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Ingénierie des protéines</term><term>Modèles moléculaires</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Exploring the vicinity around a locus of a protein in sequence space may identify homologs with enhanced properties, which could become valuable in biotechnical and other applications. A rational approach to this pursuit is the use of 'infologs', i.e. synthetic sequences with specific substitutions capturing maximal sequence information derived from the evolutionary history of the protein family. Ninety-five such infolog genes of poplar glutathione transferase were synthesized and expressed in Escherichia coli, and the catalytic activities of the proteins determined with alternative substrates. Sequence-activity relationships derived from the infologs were used to design a second set of 47 infologs in which 90% of the members exceeded wild-type properties. Two mutants, C2 (V55I/E95D/D108E/A160V) and G5 (F13L/C70A/G122E), were further functionally characterized. The activities of the infologs with the alternative substrates 1-chloro-2,4-dinitrobenzene and phenethyl isothiocyanate, subject to different chemistries, were positively correlated, indicating that the examined mutations were affecting the overall catalytic competence without major shift in substrate discrimination. By contrast, the enhanced protein expressivity observed in many of the mutants were not similarly correlated with the activities. In conclusion, small libraries of well-defined infologs can be used to systematically explore sequence space to optimize proteins in multidimensional functional space.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28967959</PMID><DateCompleted><Year>2017</Year><Month>10</Month><Day>10</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1741-0134</ISSN><JournalIssue CitedMedium="Internet"><Volume>30</Volume><Issue>8</Issue><PubDate><Year>2017</Year><Month>08</Month><Day>01</Day></PubDate></JournalIssue><Title>Protein engineering, design & selection : PEDS</Title><ISOAbbreviation>Protein Eng Des Sel</ISOAbbreviation></Journal><ArticleTitle>Exploring sequence-function space of a poplar glutathione transferase using designed information-rich gene variants.</ArticleTitle><Pagination><MedlinePgn>543-549</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/protein/gzx045</ELocationID><Abstract><AbstractText>Exploring the vicinity around a locus of a protein in sequence space may identify homologs with enhanced properties, which could become valuable in biotechnical and other applications. A rational approach to this pursuit is the use of 'infologs', i.e. synthetic sequences with specific substitutions capturing maximal sequence information derived from the evolutionary history of the protein family. Ninety-five such infolog genes of poplar glutathione transferase were synthesized and expressed in Escherichia coli, and the catalytic activities of the proteins determined with alternative substrates. Sequence-activity relationships derived from the infologs were used to design a second set of 47 infologs in which 90% of the members exceeded wild-type properties. Two mutants, C2 (V55I/E95D/D108E/A160V) and G5 (F13L/C70A/G122E), were further functionally characterized. The activities of the infologs with the alternative substrates 1-chloro-2,4-dinitrobenzene and phenethyl isothiocyanate, subject to different chemistries, were positively correlated, indicating that the examined mutations were affecting the overall catalytic competence without major shift in substrate discrimination. By contrast, the enhanced protein expressivity observed in many of the mutants were not similarly correlated with the activities. In conclusion, small libraries of well-defined infologs can be used to systematically explore sequence space to optimize proteins in multidimensional functional space.</AbstractText><CopyrightInformation>© The Author 2017. Published by Oxford University Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Musdal</LastName><ForeName>Yaman</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Neurochemistry, Arrhenius Laboratories, Stockholm University, Svante Arrhenius väg 16B, SE-10691 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Govindarajan</LastName><ForeName>Sridhar</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>ATUM, 37950 Central Ct, Newark, CA 94560, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mannervik</LastName><ForeName>Bengt</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Neurochemistry, Arrhenius Laboratories, Stockholm University, Svante Arrhenius väg 16B, SE-10691 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType 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MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015202" MajorTopicYN="N">Protein Engineering</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">alternative substrates</Keyword><Keyword MajorTopicYN="Y">directed protein evolution</Keyword><Keyword MajorTopicYN="Y">enhanced activities</Keyword><Keyword MajorTopicYN="Y">glutathione 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Musdal</name></region><name sortKey="Mannervik, Bengt" sort="Mannervik, Bengt" uniqKey="Mannervik B" first="Bengt" last="Mannervik">Bengt Mannervik</name></country><country name="États-Unis"><region name="Californie"><name sortKey="Govindarajan, Sridhar" sort="Govindarajan, Sridhar" uniqKey="Govindarajan S" first="Sridhar" last="Govindarajan">Sridhar Govindarajan</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:28967959" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PoplarV1
| This area was generated with Dilib version V0.6.37. |  |