Evolution of Protein Quaternary Structure in Response to Selective Pressure for Increased Thermostability.
Identifieur interne : 001F40 ( Main/Exploration ); précédent : 001F39; suivant : 001F41Evolution 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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Fraser</name><affiliation wicri:level="1"><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, ACT 2601, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Research School of Chemistry, Australian National University, Canberra, ACT 2601</wicri:regionArea><wicri:noRegion>ACT 2601</wicri:noRegion></affiliation></author><author><name sortKey="Liu, Jian Wei" sort="Liu, Jian Wei" uniqKey="Liu J" first="Jian-Wei" last="Liu">Jian-Wei Liu</name><affiliation wicri:level="1"><nlm:affiliation>Commonwealth Scientific and Industrial Research Organization, Land and Water Flagship, Canberra, ACT 0200, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Commonwealth Scientific and Industrial Research Organization, Land and Water Flagship, Canberra, ACT 0200</wicri:regionArea><wicri:noRegion>ACT 0200</wicri:noRegion></affiliation></author><author><name sortKey="Mabbitt, Peter D" sort="Mabbitt, Peter D" uniqKey="Mabbitt P" first="Peter D" last="Mabbitt">Peter D. Mabbitt</name><affiliation wicri:level="1"><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, ACT 2601, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Research School of Chemistry, Australian National University, Canberra, ACT 2601</wicri:regionArea><wicri:noRegion>ACT 2601</wicri:noRegion></affiliation></author><author><name sortKey="Correy, Galen J" sort="Correy, Galen J" uniqKey="Correy G" first="Galen J" last="Correy">Galen J. 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Coppin</name><affiliation wicri:level="1"><nlm:affiliation>Commonwealth Scientific and Industrial Research Organization, Land and Water Flagship, Canberra, ACT 0200, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Commonwealth Scientific and Industrial Research Organization, Land and Water Flagship, Canberra, ACT 0200</wicri:regionArea><wicri:noRegion>ACT 0200</wicri:noRegion></affiliation></author><author><name sortKey="Lethier, Mathilde" sort="Lethier, Mathilde" uniqKey="Lethier M" first="Mathilde" last="Lethier">Mathilde Lethier</name><affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Structurale, Commissariat a l'Energie Atomique, F-38027 Grenoble, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Biologie Structurale, Commissariat a l'Energie Atomique, F-38027 Grenoble</wicri:regionArea><wicri:noRegion>38027 Grenoble</wicri:noRegion><wicri:noRegion>38027 Grenoble</wicri:noRegion></affiliation></author><author><name sortKey="Perugini, Matthew A" sort="Perugini, Matthew A" uniqKey="Perugini M" first="Matthew A" last="Perugini">Matthew A. Perugini</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086</wicri:regionArea><wicri:noRegion>VIC 3086</wicri:noRegion></affiliation></author><author><name sortKey="Murphy, James M" sort="Murphy, James M" uniqKey="Murphy J" first="James M" last="Murphy">James M. Murphy</name><affiliation wicri:level="4"><nlm:affiliation>Cell Signalling and Cell Death Division, The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Melbourne, VIC 3050, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Cell Signalling and Cell Death Division, The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Melbourne, VIC 3050</wicri:regionArea><orgName type="university">Université de Melbourne</orgName><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></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 wicri:level="1"><nlm:affiliation>Commonwealth Scientific and Industrial Research Organization, Land and Water Flagship, Canberra, ACT 0200, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Commonwealth Scientific and Industrial Research Organization, Land and Water Flagship, Canberra, ACT 0200</wicri:regionArea><wicri:noRegion>ACT 0200</wicri:noRegion></affiliation></author><author><name sortKey="Weik, Martin" sort="Weik, Martin" uniqKey="Weik M" first="Martin" last="Weik">Martin Weik</name><affiliation wicri:level="1"><nlm:affiliation>Institut de Biologie Structurale, Commissariat a l'Energie Atomique, F-38027 Grenoble, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Biologie Structurale, Commissariat a l'Energie Atomique, F-38027 Grenoble</wicri:regionArea><wicri:noRegion>38027 Grenoble</wicri:noRegion><wicri:noRegion>38027 Grenoble</wicri:noRegion></affiliation></author><author><name sortKey="Jackson, Colin J" sort="Jackson, Colin J" uniqKey="Jackson C" first="Colin J" last="Jackson">Colin J. Jackson</name><affiliation wicri:level="1"><nlm:affiliation>Research School of Chemistry, Australian National University, Canberra, ACT 2601, Australia. Electronic address: cjackson@rsc.anu.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Research School of Chemistry, Australian National University, Canberra, ACT 2601</wicri:regionArea><wicri:noRegion>ACT 2601</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="eISSN">1089-8638</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Australia</term><term>Biological Evolution</term><term>Mutation (genetics)</term><term>Protein Multimerization (genetics)</term><term>Protein Structure, Quaternary</term><term>Proteins (genetics)</term><term>Sequence Alignment (methods)</term><term>Sheep (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences ()</term><term>Animaux</term><term>Australie</term><term>Multimérisation de protéines (génétique)</term><term>Mutation (génétique)</term><term>Ovis (génétique)</term><term>Protéines (génétique)</term><term>Structure quaternaire des protéines</term><term>Séquence d'acides aminés</term><term>Évolution biologique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term><term>Protein Multimerization</term><term>Sheep</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Multimérisation de protéines</term><term>Mutation</term><term>Ovis</term><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Australia</term><term>Biological Evolution</term><term>Protein Structure, Quaternary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Australie</term><term>Structure quaternaire des protéines</term><term>Séquence d'acides aminés</term><term>Évolution biologique</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><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>Pour manipuler ce document sous Unix (Dilib)
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