Evolution of Protein Quaternary Structure in Response to Selective Pressure for Increased Thermostability.
Identifieur interne : 001E90 ( PubMed/Checkpoint ); précédent : 001E89; suivant : 001E91Evolution of Protein Quaternary Structure in Response to Selective Pressure for Increased Thermostability.
Auteurs : Nicholas J. Fraser [Australie] ; Jian-Wei Liu [Australie] ; Peter D. Mabbitt [Australie] ; Galen J. Correy [Australie] ; Chris W. Coppin [Australie] ; Mathilde Lethier [France] ; Matthew A. Perugini [Australie] ; James M. Murphy [Australie] ; John G. Oakeshott [Australie] ; Martin Weik [France] ; Colin J. Jackson [Australie]Source :
- Journal of molecular biology [ 1089-8638 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Proteins.
- genetics : Mutation, Protein Multimerization, Sheep.
- methods : Sequence Alignment.
- Amino Acid Sequence, Animals, Australia, Biological Evolution, Protein Structure, Quaternary.
Abstract
Oligomerization has been suggested to be an important mechanism for increasing or maintaining the thermostability of proteins. Although it is evident that protein-protein contacts can result in substantial stabilization in many extant proteins, evidence for evolutionary selection for oligomerization is largely indirect and little is understood of the early steps in the evolution of oligomers. A laboratory-directed evolution experiment that selected for increased thermostability in the αE7 carboxylesterase from the Australian sheep blowfly, Lucilia cuprina, resulted in a thermostable variant, LcαE7-4a, that displayed increased levels of dimeric and tetrameric quaternary structure. A trade-off between activity and thermostability was made during the evolution of thermostability, with the higher-order oligomeric species displaying the greatest thermostability and lowest catalytic activity. Analysis of monomeric and dimeric LcαE7-4a crystal structures revealed that only one of the oligomerization-inducing mutations was located at a potential protein-protein interface. This work demonstrates that by imposing a selective pressure demanding greater thermostability, mutations can lead to increased oligomerization and stabilization, providing support for the hypothesis that oligomerization is a viable evolutionary strategy for protein stabilization.
DOI: 10.1016/j.jmb.2016.03.014
PubMed: 27016206
Affiliations:
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pubmed:27016206Le document en format XML
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<front><div type="abstract" xml:lang="en">Oligomerization has been suggested to be an important mechanism for increasing or maintaining the thermostability of proteins. Although it is evident that protein-protein contacts can result in substantial stabilization in many extant proteins, evidence for evolutionary selection for oligomerization is largely indirect and little is understood of the early steps in the evolution of oligomers. A laboratory-directed evolution experiment that selected for increased thermostability in the αE7 carboxylesterase from the Australian sheep blowfly, Lucilia cuprina, resulted in a thermostable variant, LcαE7-4a, that displayed increased levels of dimeric and tetrameric quaternary structure. A trade-off between activity and thermostability was made during the evolution of thermostability, with the higher-order oligomeric species displaying the greatest thermostability and lowest catalytic activity. Analysis of monomeric and dimeric LcαE7-4a crystal structures revealed that only one of the oligomerization-inducing mutations was located at a potential protein-protein interface. This work demonstrates that by imposing a selective pressure demanding greater thermostability, mutations can lead to increased oligomerization and stabilization, providing support for the hypothesis that oligomerization is a viable evolutionary strategy for protein stabilization.</div>
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<Abstract><AbstractText>Oligomerization has been suggested to be an important mechanism for increasing or maintaining the thermostability of proteins. Although it is evident that protein-protein contacts can result in substantial stabilization in many extant proteins, evidence for evolutionary selection for oligomerization is largely indirect and little is understood of the early steps in the evolution of oligomers. A laboratory-directed evolution experiment that selected for increased thermostability in the αE7 carboxylesterase from the Australian sheep blowfly, Lucilia cuprina, resulted in a thermostable variant, LcαE7-4a, that displayed increased levels of dimeric and tetrameric quaternary structure. A trade-off between activity and thermostability was made during the evolution of thermostability, with the higher-order oligomeric species displaying the greatest thermostability and lowest catalytic activity. Analysis of monomeric and dimeric LcαE7-4a crystal structures revealed that only one of the oligomerization-inducing mutations was located at a potential protein-protein interface. This work demonstrates that by imposing a selective pressure demanding greater thermostability, mutations can lead to increased oligomerization and stabilization, providing support for the hypothesis that oligomerization is a viable evolutionary strategy for protein stabilization.</AbstractText>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fraser</LastName>
<ForeName>Nicholas J</ForeName>
<Initials>NJ</Initials>
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<ForeName>Peter D</ForeName>
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<Author ValidYN="Y"><LastName>Correy</LastName>
<ForeName>Galen J</ForeName>
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</AffiliationInfo>
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<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2016</Year>
<Month>03</Month>
<Day>22</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>J Mol Biol</MedlineTA>
<NlmUniqueID>2985088R</NlmUniqueID>
<ISSNLinking>0022-2836</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011506">Proteins</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="D001315" MajorTopicYN="N">Australia</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005075" MajorTopicYN="N">Biological Evolution</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020836" MajorTopicYN="N">Protein Structure, Quaternary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName>
<QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012756" MajorTopicYN="N">Sheep</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">carboxylesterase</Keyword>
<Keyword MajorTopicYN="N">directed evolution</Keyword>
<Keyword MajorTopicYN="N">interface</Keyword>
<Keyword MajorTopicYN="N">oligomerization</Keyword>
<Keyword MajorTopicYN="N">thermostability</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year>
<Month>11</Month>
<Day>18</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2016</Year>
<Month>03</Month>
<Day>07</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2016</Year>
<Month>03</Month>
<Day>16</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2016</Year>
<Month>3</Month>
<Day>27</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2016</Year>
<Month>3</Month>
<Day>27</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2017</Year>
<Month>6</Month>
<Day>16</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">27016206</ArticleId>
<ArticleId IdType="pii">S0022-2836(16)00200-X</ArticleId>
<ArticleId IdType="doi">10.1016/j.jmb.2016.03.014</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Australie</li>
<li>France</li>
</country>
<region><li>Victoria (État)</li>
</region>
<settlement><li>Melbourne</li>
</settlement>
<orgName><li>Université de Melbourne</li>
</orgName>
</list>
<tree><country name="Australie"><noRegion><name sortKey="Fraser, Nicholas J" sort="Fraser, Nicholas J" uniqKey="Fraser N" first="Nicholas J" last="Fraser">Nicholas J. Fraser</name>
</noRegion>
<name sortKey="Coppin, Chris W" sort="Coppin, Chris W" uniqKey="Coppin C" first="Chris W" last="Coppin">Chris W. Coppin</name>
<name sortKey="Correy, Galen J" sort="Correy, Galen J" uniqKey="Correy G" first="Galen J" last="Correy">Galen J. Correy</name>
<name sortKey="Jackson, Colin J" sort="Jackson, Colin J" uniqKey="Jackson C" first="Colin J" last="Jackson">Colin J. Jackson</name>
<name sortKey="Liu, Jian Wei" sort="Liu, Jian Wei" uniqKey="Liu J" first="Jian-Wei" last="Liu">Jian-Wei Liu</name>
<name sortKey="Mabbitt, Peter D" sort="Mabbitt, Peter D" uniqKey="Mabbitt P" first="Peter D" last="Mabbitt">Peter D. Mabbitt</name>
<name sortKey="Murphy, James M" sort="Murphy, James M" uniqKey="Murphy J" first="James M" last="Murphy">James M. Murphy</name>
<name sortKey="Oakeshott, John G" sort="Oakeshott, John G" uniqKey="Oakeshott J" first="John G" last="Oakeshott">John G. Oakeshott</name>
<name sortKey="Perugini, Matthew A" sort="Perugini, Matthew A" uniqKey="Perugini M" first="Matthew A" last="Perugini">Matthew A. Perugini</name>
</country>
<country name="France"><noRegion><name sortKey="Lethier, Mathilde" sort="Lethier, Mathilde" uniqKey="Lethier M" first="Mathilde" last="Lethier">Mathilde Lethier</name>
</noRegion>
<name sortKey="Weik, Martin" sort="Weik, Martin" uniqKey="Weik M" first="Martin" last="Weik">Martin Weik</name>
</country>
</tree>
</affiliations>
</record>
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