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Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.

Identifieur interne : 001C25 ( PubMed/Checkpoint ); précédent : 001C24; suivant : 001C26

Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.

Auteurs : Oliver W. Bayfield [Royaume-Uni] ; Chao-Sheng Chen ; Andrea R. Patterson ; Weisha Luan ; Callum Smits ; Paul Gollnick ; Alfred A. Antson

Source :

PloS one [ 1932-6203 ] ; 2012.

RBID : pubmed:22970197

Descripteurs français

English descriptors

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 Bacilli, 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.

DOI: 10.1371/journal.pone.0044309
PubMed: 22970197

Affiliations:

Royaume-Uni

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<term>Kinetics</term>
<term>Mass Spectrometry</term>
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<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>
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<term>Transcription Factors</term>
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<term>Tryptophan</term>
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<term>Cristallographie aux rayons X</term>
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<term>Protéines de liaison à l'ARN</term>
<term>Protéines mutantes</term>
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<front><div type="abstract" xml:lang="en">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 Bacilli, 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.</div>
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<DateCompleted><Year>2013</Year>
<Month>05</Month>
<Day>01</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
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<JournalIssue CitedMedium="Internet"><Volume>7</Volume>
<Issue>9</Issue>
<PubDate><Year>2012</Year>
</PubDate>
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<Title>PloS one</Title>
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<ArticleTitle>Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.</ArticleTitle>
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<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">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 Bacilli, 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.</AbstractText>
<AbstractText Label="METHODOLOGY/PRINCIPAL FINDINGS" NlmCategory="RESULTS">Among the wild type B. stearothermophilus, B. halodurans and B. subtilis 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 B. subtilis S72N TRAP.</AbstractText>
<AbstractText Label="CONCLUSIONS/SIGNIFICANCE" NlmCategory="CONCLUSIONS">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.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bayfield</LastName>
<ForeName>Oliver W</ForeName>
<Initials>OW</Initials>
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<ForeName>Chao-Sheng</ForeName>
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<Author ValidYN="Y"><LastName>Patterson</LastName>
<ForeName>Andrea R</ForeName>
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<Author ValidYN="Y"><LastName>Smits</LastName>
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<Author ValidYN="Y"><LastName>Gollnick</LastName>
<ForeName>Paul</ForeName>
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<Author ValidYN="Y"><LastName>Antson</LastName>
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<tree><noCountry><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="Gollnick, Paul" sort="Gollnick, Paul" uniqKey="Gollnick P" first="Paul" last="Gollnick">Paul Gollnick</name>
<name sortKey="Luan, Weisha" sort="Luan, Weisha" uniqKey="Luan W" first="Weisha" last="Luan">Weisha Luan</name>
<name sortKey="Patterson, Andrea R" sort="Patterson, Andrea R" uniqKey="Patterson A" first="Andrea R" last="Patterson">Andrea R. Patterson</name>
<name sortKey="Smits, Callum" sort="Smits, Callum" uniqKey="Smits C" first="Callum" last="Smits">Callum Smits</name>
</noCountry>
<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>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Checkpoint

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001C25 | SxmlIndent | more

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Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    MersV1
   |flux=    PubMed
   |étape=   Checkpoint
   |type=    RBID
   |clé=     pubmed:22970197
   |texte=   Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/RBID.i   -Sk "pubmed:22970197" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd   \
       | NlmPubMed2Wicri -a MersV1

This area was generated with Dilib version V0.6.33.
Data generation: Mon Apr 20 23:26:43 2020. Site generation: Sat Mar 27 09:06:09 2021

	Serveur d'exploration MERS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration MERS

Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.

Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.

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Abstract

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Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki