300-Fold increase in production of the Zn2+-dependent dechlorinase TrzN in soluble form via apoenzyme stabilization.
Identifieur interne : 003624 ( PubMed/Corpus ); précédent : 003623; suivant : 003625300-Fold increase in production of the Zn2+-dependent dechlorinase TrzN in soluble form via apoenzyme stabilization.
Auteurs : Colin J. Jackson ; Christopher W. Coppin ; Paul D. Carr ; Alexey Aleksandrov ; Matthew Wilding ; Elena Sugrue ; Joanna Ubels ; Michael Paks ; Janet Newman ; Thomas S. Peat ; Robyn J. Russell ; Martin Field ; Martin Weik ; John G. Oakeshott ; Colin ScottSource :
- Applied and environmental microbiology [ 1098-5336 ] ; 2014.
English descriptors
- KwdEn :
- Apoenzymes (biosynthesis), Apoenzymes (chemistry), Apoenzymes (genetics), Arthrobacter (enzymology), Computer Simulation, Crystallography, X-Ray, Enzyme Stability, Escherichia coli (enzymology), Escherichia coli (metabolism), Herbicides (metabolism), Hydrolases (biosynthesis), Hydrolases (chemistry), Hydrolases (genetics), Hydrolysis, Kinetics, Models, Molecular, Mutant Proteins (biosynthesis), Mutant Proteins (chemistry), Mutant Proteins (genetics), Mutation, Missense, Protein Conformation, Recombinant Proteins (biosynthesis), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Solubility, Triazines (metabolism).
- MESH :
- chemical , biosynthesis : Apoenzymes, Hydrolases, Mutant Proteins, Recombinant Proteins.
- chemical , chemistry : Apoenzymes, Hydrolases, Mutant Proteins, Recombinant Proteins.
- chemical , genetics : Apoenzymes, Hydrolases, Mutant Proteins, Recombinant Proteins.
- enzymology : Arthrobacter, Escherichia coli.
- metabolism : Escherichia coli, Herbicides, Triazines.
- Computer Simulation, Crystallography, X-Ray, Enzyme Stability, Hydrolysis, Kinetics, Models, Molecular, Mutation, Missense, Protein Conformation, Solubility.
Abstract
Microbial metalloenzymes constitute a large library of biocatalysts, a number of which have already been shown to catalyze the breakdown of toxic chemicals or industrially relevant chemical transformations. However, while there is considerable interest in harnessing these catalysts for biotechnology, for many of the enzymes, their large-scale production in active, soluble form in recombinant systems is a significant barrier to their use. In this work, we demonstrate that as few as three mutations can result in a 300-fold increase in the expression of soluble TrzN, an enzyme from Arthrobacter aurescens with environmental applications that catalyzes the hydrolysis of triazine herbicides, in Escherichia coli. Using a combination of X-ray crystallography, kinetic analysis, and computational simulation, we show that the majority of the improvement in expression is due to stabilization of the apoenzyme rather than the metal ion-bound holoenzyme. This provides a structural and mechanistic explanation for the observation that many compensatory mutations can increase levels of soluble-protein production without increasing the stability of the final, active form of the enzyme. This study provides a molecular understanding of the importance of the stability of metal ion free states to the accumulation of soluble protein and shows that differences between apoenzyme and holoenzyme structures can result in mutations affecting the stability of either state differently.
DOI: 10.1128/AEM.00916-14
PubMed: 24771025
Links to Exploration step
pubmed:24771025Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">300-Fold increase in production of the Zn2+-dependent dechlorinase TrzN in soluble form via apoenzyme stabilization.</title><author><name sortKey="Jackson, Colin J" sort="Jackson, Colin J" uniqKey="Jackson C" first="Colin J" last="Jackson">Colin J. Jackson</name><affiliation><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia Institut de Biologie Structurale, Grenoble, France colin.jackson@anu.edu.au colin.scott@csiro.au.</nlm:affiliation></affiliation></author><author><name sortKey="Coppin, Christopher W" sort="Coppin, Christopher W" uniqKey="Coppin C" first="Christopher W" last="Coppin">Christopher W. Coppin</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Carr, Paul D" sort="Carr, Paul D" uniqKey="Carr P" first="Paul D" last="Carr">Paul D. Carr</name><affiliation><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Aleksandrov, Alexey" sort="Aleksandrov, Alexey" uniqKey="Aleksandrov A" first="Alexey" last="Aleksandrov">Alexey Aleksandrov</name><affiliation><nlm:affiliation>Institut de Biologie Structurale, Grenoble, France.</nlm:affiliation></affiliation></author><author><name sortKey="Wilding, Matthew" sort="Wilding, Matthew" uniqKey="Wilding M" first="Matthew" last="Wilding">Matthew Wilding</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Sugrue, Elena" sort="Sugrue, Elena" uniqKey="Sugrue E" first="Elena" last="Sugrue">Elena Sugrue</name><affiliation><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Ubels, Joanna" sort="Ubels, Joanna" uniqKey="Ubels J" first="Joanna" last="Ubels">Joanna Ubels</name><affiliation><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Paks, Michael" sort="Paks, Michael" uniqKey="Paks M" first="Michael" last="Paks">Michael Paks</name><affiliation><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Newman, Janet" sort="Newman, Janet" uniqKey="Newman J" first="Janet" last="Newman">Janet Newman</name><affiliation><nlm:affiliation>CSIRO Materials, Science and Engineering, Parkville, Victoria, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Peat, Thomas S" sort="Peat, Thomas S" uniqKey="Peat T" first="Thomas S" last="Peat">Thomas S. 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Oakeshott</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Scott, Colin" sort="Scott, Colin" uniqKey="Scott C" first="Colin" last="Scott">Colin Scott</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia colin.jackson@anu.edu.au colin.scott@csiro.au.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:24771025</idno><idno type="pmid">24771025</idno><idno type="doi">10.1128/AEM.00916-14</idno><idno type="wicri:Area/PubMed/Corpus">003624</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003624</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">300-Fold increase in production of the Zn2+-dependent dechlorinase TrzN in soluble form via apoenzyme stabilization.</title><author><name sortKey="Jackson, Colin J" sort="Jackson, Colin J" uniqKey="Jackson C" first="Colin J" last="Jackson">Colin J. Jackson</name><affiliation><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia Institut de Biologie Structurale, Grenoble, France colin.jackson@anu.edu.au colin.scott@csiro.au.</nlm:affiliation></affiliation></author><author><name sortKey="Coppin, Christopher W" sort="Coppin, Christopher W" uniqKey="Coppin C" first="Christopher W" last="Coppin">Christopher W. Coppin</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Carr, Paul D" sort="Carr, Paul D" uniqKey="Carr P" first="Paul D" last="Carr">Paul D. Carr</name><affiliation><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Aleksandrov, Alexey" sort="Aleksandrov, Alexey" uniqKey="Aleksandrov A" first="Alexey" last="Aleksandrov">Alexey Aleksandrov</name><affiliation><nlm:affiliation>Institut de Biologie Structurale, Grenoble, France.</nlm:affiliation></affiliation></author><author><name sortKey="Wilding, Matthew" sort="Wilding, Matthew" uniqKey="Wilding M" first="Matthew" last="Wilding">Matthew Wilding</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Sugrue, Elena" sort="Sugrue, Elena" uniqKey="Sugrue E" first="Elena" last="Sugrue">Elena Sugrue</name><affiliation><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Ubels, Joanna" sort="Ubels, Joanna" uniqKey="Ubels J" first="Joanna" last="Ubels">Joanna Ubels</name><affiliation><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Paks, Michael" sort="Paks, Michael" uniqKey="Paks M" first="Michael" last="Paks">Michael Paks</name><affiliation><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Newman, Janet" sort="Newman, Janet" uniqKey="Newman J" first="Janet" last="Newman">Janet Newman</name><affiliation><nlm:affiliation>CSIRO Materials, Science and Engineering, Parkville, Victoria, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Peat, Thomas S" sort="Peat, Thomas S" uniqKey="Peat T" first="Thomas S" last="Peat">Thomas S. Peat</name><affiliation><nlm:affiliation>CSIRO Materials, Science and Engineering, Parkville, Victoria, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Russell, Robyn J" sort="Russell, Robyn J" uniqKey="Russell R" first="Robyn J" last="Russell">Robyn J. Russell</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Field, Martin" sort="Field, Martin" uniqKey="Field M" first="Martin" last="Field">Martin Field</name><affiliation><nlm:affiliation>Institut de Biologie Structurale, Grenoble, France.</nlm:affiliation></affiliation></author><author><name sortKey="Weik, Martin" sort="Weik, Martin" uniqKey="Weik M" first="Martin" last="Weik">Martin Weik</name><affiliation><nlm:affiliation>Institut de Biologie Structurale, Grenoble, France.</nlm:affiliation></affiliation></author><author><name sortKey="Oakeshott, John G" sort="Oakeshott, John G" uniqKey="Oakeshott J" first="John G" last="Oakeshott">John G. Oakeshott</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Scott, Colin" sort="Scott, Colin" uniqKey="Scott C" first="Colin" last="Scott">Colin Scott</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia colin.jackson@anu.edu.au colin.scott@csiro.au.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Applied and environmental microbiology</title><idno type="eISSN">1098-5336</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Apoenzymes (biosynthesis)</term><term>Apoenzymes (chemistry)</term><term>Apoenzymes (genetics)</term><term>Arthrobacter (enzymology)</term><term>Computer Simulation</term><term>Crystallography, X-Ray</term><term>Enzyme Stability</term><term>Escherichia coli (enzymology)</term><term>Escherichia coli (metabolism)</term><term>Herbicides (metabolism)</term><term>Hydrolases (biosynthesis)</term><term>Hydrolases (chemistry)</term><term>Hydrolases (genetics)</term><term>Hydrolysis</term><term>Kinetics</term><term>Models, Molecular</term><term>Mutant Proteins (biosynthesis)</term><term>Mutant Proteins (chemistry)</term><term>Mutant Proteins (genetics)</term><term>Mutation, Missense</term><term>Protein Conformation</term><term>Recombinant Proteins (biosynthesis)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Solubility</term><term>Triazines (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Apoenzymes</term><term>Hydrolases</term><term>Mutant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Apoenzymes</term><term>Hydrolases</term><term>Mutant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Apoenzymes</term><term>Hydrolases</term><term>Mutant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arthrobacter</term><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Herbicides</term><term>Triazines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Computer Simulation</term><term>Crystallography, X-Ray</term><term>Enzyme Stability</term><term>Hydrolysis</term><term>Kinetics</term><term>Models, Molecular</term><term>Mutation, Missense</term><term>Protein Conformation</term><term>Solubility</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Microbial metalloenzymes constitute a large library of biocatalysts, a number of which have already been shown to catalyze the breakdown of toxic chemicals or industrially relevant chemical transformations. However, while there is considerable interest in harnessing these catalysts for biotechnology, for many of the enzymes, their large-scale production in active, soluble form in recombinant systems is a significant barrier to their use. In this work, we demonstrate that as few as three mutations can result in a 300-fold increase in the expression of soluble TrzN, an enzyme from Arthrobacter aurescens with environmental applications that catalyzes the hydrolysis of triazine herbicides, in Escherichia coli. Using a combination of X-ray crystallography, kinetic analysis, and computational simulation, we show that the majority of the improvement in expression is due to stabilization of the apoenzyme rather than the metal ion-bound holoenzyme. This provides a structural and mechanistic explanation for the observation that many compensatory mutations can increase levels of soluble-protein production without increasing the stability of the final, active form of the enzyme. This study provides a molecular understanding of the importance of the stability of metal ion free states to the accumulation of soluble protein and shows that differences between apoenzyme and holoenzyme structures can result in mutations affecting the stability of either state differently.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24771025</PMID><DateCreated><Year>2014</Year><Month>07</Month><Day>29</Day></DateCreated><DateCompleted><Year>2015</Year><Month>03</Month><Day>30</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5336</ISSN><JournalIssue CitedMedium="Internet"><Volume>80</Volume><Issue>13</Issue><PubDate><Year>2014</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl. Environ. Microbiol.</ISOAbbreviation></Journal><ArticleTitle>300-Fold increase in production of the Zn2+-dependent dechlorinase TrzN in soluble form via apoenzyme stabilization.</ArticleTitle><Pagination><MedlinePgn>4003-11</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/AEM.00916-14</ELocationID><Abstract><AbstractText>Microbial metalloenzymes constitute a large library of biocatalysts, a number of which have already been shown to catalyze the breakdown of toxic chemicals or industrially relevant chemical transformations. However, while there is considerable interest in harnessing these catalysts for biotechnology, for many of the enzymes, their large-scale production in active, soluble form in recombinant systems is a significant barrier to their use. In this work, we demonstrate that as few as three mutations can result in a 300-fold increase in the expression of soluble TrzN, an enzyme from Arthrobacter aurescens with environmental applications that catalyzes the hydrolysis of triazine herbicides, in Escherichia coli. Using a combination of X-ray crystallography, kinetic analysis, and computational simulation, we show that the majority of the improvement in expression is due to stabilization of the apoenzyme rather than the metal ion-bound holoenzyme. This provides a structural and mechanistic explanation for the observation that many compensatory mutations can increase levels of soluble-protein production without increasing the stability of the final, active form of the enzyme. This study provides a molecular understanding of the importance of the stability of metal ion free states to the accumulation of soluble protein and shows that differences between apoenzyme and holoenzyme structures can result in mutations affecting the stability of either state differently.</AbstractText><CopyrightInformation>Copyright © 2014, American Society for Microbiology. All Rights Reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jackson</LastName><ForeName>Colin J</ForeName><Initials>CJ</Initials><AffiliationInfo><Affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia Institut de Biologie Structurale, Grenoble, France colin.jackson@anu.edu.au colin.scott@csiro.au.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Coppin</LastName><ForeName>Christopher W</ForeName><Initials>CW</Initials><AffiliationInfo><Affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Carr</LastName><ForeName>Paul D</ForeName><Initials>PD</Initials><AffiliationInfo><Affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aleksandrov</LastName><ForeName>Alexey</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institut de Biologie Structurale, Grenoble, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wilding</LastName><ForeName>Matthew</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sugrue</LastName><ForeName>Elena</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ubels</LastName><ForeName>Joanna</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Paks</LastName><ForeName>Michael</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Research School of Chemistry, Australian National University, Canberra, Australian Capital Territory, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Newman</LastName><ForeName>Janet</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>CSIRO Materials, Science and Engineering, Parkville, Victoria, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Peat</LastName><ForeName>Thomas S</ForeName><Initials>TS</Initials><AffiliationInfo><Affiliation>CSIRO Materials, Science and Engineering, Parkville, Victoria, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Russell</LastName><ForeName>Robyn J</ForeName><Initials>RJ</Initials><AffiliationInfo><Affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Field</LastName><ForeName>Martin</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institut de Biologie Structurale, Grenoble, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Weik</LastName><ForeName>Martin</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institut de Biologie Structurale, Grenoble, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oakeshott</LastName><ForeName>John G</ForeName><Initials>JG</Initials><AffiliationInfo><Affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, Australian Capital Territory, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Scott</LastName><ForeName>Colin</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>CSIRO Ecosystems Sciences, Black Mountain, Canberra, 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