Trp RNA-Binding Attenuation Protein: Modifying Symmetry and Stability of a Circular Oligomer
Identifieur interne : 002286 ( Main/Exploration ); précédent : 002285; suivant : 002287Trp RNA-Binding Attenuation Protein: Modifying Symmetry and Stability of a Circular Oligomer
Auteurs : Oliver W. Bayfield [Royaume-Uni] ; Chao-Sheng Chen [Royaume-Uni] ; Andrea R. Patterson [États-Unis] ; Weisha Luan [Royaume-Uni] ; Callum Smits [Royaume-Uni] ; Paul Gollnick [États-Unis] ; Alfred A. Antson [Royaume-Uni]Source :
- PLoS ONE [ 1932-6203 ] ; 2012.
Descripteurs français
- KwdFr :
- Bacillus subtilis (métabolisme), Cinétique, Cristallographie aux rayons X, Facteurs de transcription (), Facteurs de transcription (métabolisme), Liaison aux protéines, Protéines bactériennes (), Protéines bactériennes (métabolisme), Protéines de liaison à l'ARN (), Protéines de liaison à l'ARN (métabolisme), Protéines mutantes (), Protéines mutantes (métabolisme), Sous-unités de protéines (), Spectrométrie de masse, Stabilité protéique, Structure quaternaire des protéines, Structure secondaire des protéines, Température de transition, Tryptophane (métabolisme).
- MESH :
- métabolisme : Bacillus subtilis, Facteurs de transcription, Protéines bactériennes, Protéines de liaison à l'ARN, Protéines mutantes, Tryptophane.
- Cinétique, Cristallographie aux rayons X, Facteurs de transcription, Liaison aux protéines, Protéines bactériennes, Protéines de liaison à l'ARN, Protéines mutantes, Sous-unités de protéines, Spectrométrie de masse, Stabilité protéique, Structure quaternaire des protéines, Structure secondaire des protéines, Température de transition.
English descriptors
- KwdEn :
- Bacillus subtilis (metabolism), Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Crystallography, X-Ray, Kinetics, Mass Spectrometry, Mutant Proteins (chemistry), Mutant Proteins (metabolism), Protein Binding, Protein Stability, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Subunits (chemistry), RNA-Binding Proteins (chemistry), RNA-Binding Proteins (metabolism), Transcription Factors (chemistry), Transcription Factors (metabolism), Transition Temperature, Tryptophan (metabolism).
- MESH :
- chemical , chemistry : Bacterial Proteins, Mutant Proteins, Protein Subunits, RNA-Binding Proteins, Transcription Factors.
- metabolism : Bacillus subtilis, Bacterial Proteins, Mutant Proteins, RNA-Binding Proteins, Transcription Factors, Tryptophan.
- Crystallography, X-Ray, Kinetics, Mass Spectrometry, Protein Binding, Protein Stability, Protein Structure, Quaternary, Protein Structure, Secondary, Transition Temperature.
Abstract
Subunit number is amongst the most important structural parameters that determine size, symmetry and geometry of a circular protein oligomer. The L-tryptophan biosynthesis regulator, TRAP, present in several
Among the wild type
We conclude that the oligomeric state of a circular protein can be changed by introducing a point mutation at a subunit interface. Exclusion (or deletion) of the C-terminus from the subunit interface has a major impact on properties of TRAP oligomers, making them more stable, and we argue that the cause of these changes is the altered oligomeric state. The more stable TRAP oligomers could be used in potential applications of TRAP in bionanotechnology.
Url:
DOI: 10.1371/journal.pone.0044309
PubMed: 22970197
PubMed Central: 3435397
Affiliations:
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Le document en format XML
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Bayfield</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>York Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom</addr-line></nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>York Structural Biology Laboratory, Department of Chemistry, University of York, York</wicri:regionArea><wicri:noRegion>York</wicri:noRegion></affiliation></author><author><name sortKey="Chen, Chao Sheng" sort="Chen, Chao Sheng" uniqKey="Chen C" first="Chao-Sheng" last="Chen">Chao-Sheng Chen</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>York Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom</addr-line></nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>York Structural Biology Laboratory, Department of Chemistry, University of York, York</wicri:regionArea><wicri:noRegion>York</wicri:noRegion></affiliation></author><author><name sortKey="Patterson, Andrea R" sort="Patterson, Andrea R" uniqKey="Patterson A" first="Andrea R." last="Patterson">Andrea R. Patterson</name><affiliation wicri:level="2"><nlm:aff id="aff2"><addr-line>Department of Biological Sciences, State University of New York, Buffalo, New York, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, State University of New York, Buffalo, New York</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></affiliation></author><author><name sortKey="Luan, Weisha" sort="Luan, Weisha" uniqKey="Luan W" first="Weisha" last="Luan">Weisha Luan</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>York Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom</addr-line></nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>York Structural Biology Laboratory, Department of Chemistry, University of York, York</wicri:regionArea><wicri:noRegion>York</wicri:noRegion></affiliation></author><author><name sortKey="Smits, Callum" sort="Smits, Callum" uniqKey="Smits C" first="Callum" last="Smits">Callum Smits</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>York Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom</addr-line></nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>York Structural Biology Laboratory, Department of Chemistry, University of York, York</wicri:regionArea><wicri:noRegion>York</wicri:noRegion></affiliation></author><author><name sortKey="Gollnick, Paul" sort="Gollnick, Paul" uniqKey="Gollnick P" first="Paul" last="Gollnick">Paul Gollnick</name><affiliation wicri:level="2"><nlm:aff id="aff2"><addr-line>Department of Biological Sciences, State University of New York, Buffalo, New York, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, State University of New York, Buffalo, New York</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></affiliation></author><author><name sortKey="Antson, Alfred A" sort="Antson, Alfred A" uniqKey="Antson A" first="Alfred A." last="Antson">Alfred A. Antson</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>York Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom</addr-line></nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>York Structural Biology Laboratory, Department of Chemistry, University of York, York</wicri:regionArea><wicri:noRegion>York</wicri:noRegion></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacillus subtilis (metabolism)</term><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (metabolism)</term><term>Crystallography, X-Ray</term><term>Kinetics</term><term>Mass Spectrometry</term><term>Mutant Proteins (chemistry)</term><term>Mutant Proteins (metabolism)</term><term>Protein Binding</term><term>Protein Stability</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Protein Subunits (chemistry)</term><term>RNA-Binding Proteins (chemistry)</term><term>RNA-Binding Proteins (metabolism)</term><term>Transcription Factors (chemistry)</term><term>Transcription Factors (metabolism)</term><term>Transition Temperature</term><term>Tryptophan (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Bacillus subtilis (métabolisme)</term><term>Cinétique</term><term>Cristallographie aux rayons X</term><term>Facteurs de transcription ()</term><term>Facteurs de transcription (métabolisme)</term><term>Liaison aux protéines</term><term>Protéines bactériennes ()</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines de liaison à l'ARN ()</term><term>Protéines de liaison à l'ARN (métabolisme)</term><term>Protéines mutantes ()</term><term>Protéines mutantes (métabolisme)</term><term>Sous-unités de protéines ()</term><term>Spectrométrie de masse</term><term>Stabilité protéique</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term><term>Température de transition</term><term>Tryptophane (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>Mutant Proteins</term><term>Protein Subunits</term><term>RNA-Binding Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Bacillus subtilis</term><term>Bacterial Proteins</term><term>Mutant Proteins</term><term>RNA-Binding Proteins</term><term>Transcription Factors</term><term>Tryptophan</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Bacillus subtilis</term><term>Facteurs de transcription</term><term>Protéines bactériennes</term><term>Protéines de liaison à l'ARN</term><term>Protéines mutantes</term><term>Tryptophane</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallography, X-Ray</term><term>Kinetics</term><term>Mass Spectrometry</term><term>Protein Binding</term><term>Protein Stability</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Transition Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Cristallographie aux rayons X</term><term>Facteurs de transcription</term><term>Liaison aux protéines</term><term>Protéines bactériennes</term><term>Protéines de liaison à l'ARN</term><term>Protéines mutantes</term><term>Sous-unités de protéines</term><term>Spectrométrie de masse</term><term>Stabilité protéique</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term><term>Température de transition</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec><title>Background</title><p>Subunit number is amongst the most important structural parameters that determine size, symmetry and geometry of a circular protein oligomer. The L-tryptophan biosynthesis regulator, TRAP, present in several <italic>Bacilli</italic>, is a good model system for investigating determinants of the oligomeric state. A short segment of C-terminal residues defines whether TRAP forms an 11-mer or 12-mer assembly. To understand which oligomeric state is more stable, we examine the stability of several wild type and mutant TRAP proteins.</p></sec><sec><title>Methodology/Principal Findings</title><p>Among the wild type <italic>B. stearothermophilus</italic>, <italic>B. halodurans</italic> and <italic>B. subtilis</italic> TRAP, we find that the former is the most stable whilst the latter is the least. Thermal stability of all TRAP is shown to increase with L-tryptophan concentration. We also find that mutant TRAP molecules that are truncated at the C-terminus - and hence induced to form 12-mers, distinct from their 11-mer wild type counterparts - have increased melting temperatures. We show that the same effect can be achieved by a point mutation S72N at a subunit interface, which leads to exclusion of C-terminal residues from the interface. Our findings are supported by dye-based scanning fluorimetry, CD spectroscopy, and by crystal structure and mass spectrometry analysis of the <italic>B. subtilis</italic> S72N TRAP.</p></sec><sec><title>Conclusions/Significance</title><p>We conclude that the oligomeric state of a circular protein can be changed by introducing a point mutation at a subunit interface. Exclusion (or deletion) of the C-terminus from the subunit interface has a major impact on properties of TRAP oligomers, making them more stable, and we argue that the cause of these changes is the altered oligomeric state. The more stable TRAP oligomers could be used in potential applications of TRAP in bionanotechnology.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Minamino, T" uniqKey="Minamino T">T Minamino</name></author><author><name sortKey="Imada, K" uniqKey="Imada K">K Imada</name></author><author><name sortKey="Kinoshita, M" uniqKey="Kinoshita M">M Kinoshita</name></author><author><name sortKey="Nakamura, S" uniqKey="Nakamura S">S Nakamura</name></author><author><name sortKey="Morimoto, Yv" uniqKey="Morimoto Y">YV Morimoto</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Weber, J" uniqKey="Weber J">J Weber</name></author><author><name sortKey="Senior, Ae" uniqKey="Senior A">AE Senior</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rao, Vb" uniqKey="Rao V">VB Rao</name></author><author><name sortKey="Feiss, M" uniqKey="Feiss M">M 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sortKey="Ericsson, Ub" uniqKey="Ericsson U">UB Ericsson</name></author><author><name sortKey="Hallberg, Bm" uniqKey="Hallberg B">BM Hallberg</name></author><author><name sortKey="Detitta, Gt" uniqKey="Detitta G">GT DeTitta</name></author><author><name sortKey="Dekker, N" uniqKey="Dekker N">N Dekker</name></author><author><name sortKey="Nordlund, P" uniqKey="Nordlund P">P Nordlund</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Li, Ptx" uniqKey="Li P">PTX Li</name></author><author><name sortKey="Gollnick, P" uniqKey="Gollnick P">P Gollnick</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>Royaume-Uni</li><li>États-Unis</li></country><region><li>État de New York</li></region></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Bayfield, Oliver W" sort="Bayfield, Oliver W" uniqKey="Bayfield O" first="Oliver W." last="Bayfield">Oliver W. Bayfield</name></noRegion><name sortKey="Antson, Alfred A" sort="Antson, Alfred A" uniqKey="Antson A" first="Alfred A." last="Antson">Alfred A. Antson</name><name sortKey="Chen, Chao Sheng" sort="Chen, Chao Sheng" uniqKey="Chen C" first="Chao-Sheng" last="Chen">Chao-Sheng Chen</name><name sortKey="Luan, Weisha" sort="Luan, Weisha" uniqKey="Luan W" first="Weisha" last="Luan">Weisha Luan</name><name sortKey="Smits, Callum" sort="Smits, Callum" uniqKey="Smits C" first="Callum" last="Smits">Callum Smits</name></country><country name="États-Unis"><region name="État de New York"><name sortKey="Patterson, Andrea R" sort="Patterson, Andrea R" uniqKey="Patterson A" first="Andrea R." last="Patterson">Andrea R. Patterson</name></region><name sortKey="Gollnick, Paul" sort="Gollnick, Paul" uniqKey="Gollnick P" first="Paul" last="Gollnick">Paul Gollnick</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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