Interaction of the trp RNA-binding attenuation protein (TRAP) with anti-TRAP.
Identifieur interne : 003055 ( Main/Exploration ); précédent : 003054; suivant : 003056Interaction of the trp RNA-binding attenuation protein (TRAP) with anti-TRAP.
Auteurs : Doug Snyder [États-Unis] ; Jeffrey Lary ; Yanling Chen ; Paul Gollnick ; James L. ColeSource :
- Journal of molecular biology [ 0022-2836 ] ; 2004.
Descripteurs français
- KwdFr :
- Bacillus subtilis (métabolisme), Facteurs de transcription (), Facteurs de transcription (métabolisme), Liaison aux protéines, Modèles moléculaires, Protéines bactériennes (), Protéines bactériennes (métabolisme), Protéines de liaison à l'ARN (), Protéines de liaison à l'ARN (métabolisme), Structures macromoléculaires, Tryptophane (métabolisme), Ultracentrifugation.
- MESH :
- métabolisme : Bacillus subtilis, Facteurs de transcription, Protéines bactériennes, Protéines de liaison à l'ARN, Tryptophane.
- Facteurs de transcription, Liaison aux protéines, Modèles moléculaires, Protéines bactériennes, Protéines de liaison à l'ARN, Structures macromoléculaires, Ultracentrifugation.
English descriptors
- KwdEn :
- Bacillus subtilis (metabolism), Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Macromolecular Substances, Models, Molecular, Protein Binding, RNA-Binding Proteins (chemistry), RNA-Binding Proteins (metabolism), Transcription Factors (chemistry), Transcription Factors (metabolism), Tryptophan (metabolism), Ultracentrifugation.
- MESH :
- chemical , chemistry : Bacterial Proteins, RNA-Binding Proteins, Transcription Factors.
- metabolism : Bacillus subtilis, Bacterial Proteins, RNA-Binding Proteins, Transcription Factors, Tryptophan.
- chemical : Macromolecular Substances, Models, Molecular, Protein Binding, Ultracentrifugation.
Abstract
The trp RNA-binding attenuation protein (TRAP) negatively regulates expression of the tryptophan biosynthesis genes of Bacillus subtilis. In the presence of tryptophan, TRAP is activated to bind to the 5'-leader region of the trp mRNA resulting in termination prior to the structural genes. In addition, accumulation of uncharged tRNA(Trp) induces synthesis of anti-TRAP (AT), which binds to TRAP and inhibits its function. Both of these proteins consist of oligomers of identical subunits. Here, we characterize the self-association of each of these proteins and the TRAP-AT interaction in free solution using equilibrium and velocity analytical ultracentrifugation. TRAP exists as a stable 11-mer in the absence and in the presence of tryptophan. Tryptophan binding induces a conformational change in TRAP. AT exists in a reversible equilibrium between trimer and dodecamer with an equilibrium constant of approximately 3 x 10(14)M(-3). About 20% of the trimer is incompetent to form dodecamer. The AT equilibrium is slow on the time-scale of the velocity experiment. Formation of TRAP-AT complexes occurs only in the presence of tryptophan. A complex containing one TRAP 11-mer and one AT 12-mer forms with high affinity. At higher ratios of TRAP:AT complexes containing two TRAP 11-mers and one AT 12-mer are detected. A model for the structure of the complex is proposed.
DOI: 10.1016/j.jmb.2004.03.030
PubMed: 15099736
Affiliations:
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Eagleville Road, U-3125, Storrs, CT 06269, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular and Cell Biology, University of Connecticut, 91 N. Eagleville Road, U-3125, Storrs, CT 06269</wicri:regionArea><placeName><region type="state">Connecticut</region></placeName></affiliation></author><author><name sortKey="Lary, Jeffrey" sort="Lary, Jeffrey" uniqKey="Lary J" first="Jeffrey" last="Lary">Jeffrey Lary</name></author><author><name sortKey="Chen, Yanling" sort="Chen, Yanling" uniqKey="Chen Y" first="Yanling" last="Chen">Yanling Chen</name></author><author><name sortKey="Gollnick, Paul" sort="Gollnick, Paul" uniqKey="Gollnick P" first="Paul" last="Gollnick">Paul Gollnick</name></author><author><name sortKey="Cole, James L" sort="Cole, James L" uniqKey="Cole J" first="James L" last="Cole">James L. Cole</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="ISSN">0022-2836</idno><imprint><date when="2004" type="published">2004</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>Macromolecular Substances</term><term>Models, Molecular</term><term>Protein Binding</term><term>RNA-Binding Proteins (chemistry)</term><term>RNA-Binding Proteins (metabolism)</term><term>Transcription Factors (chemistry)</term><term>Transcription Factors (metabolism)</term><term>Tryptophan (metabolism)</term><term>Ultracentrifugation</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Bacillus subtilis (métabolisme)</term><term>Facteurs de transcription ()</term><term>Facteurs de transcription (métabolisme)</term><term>Liaison aux protéines</term><term>Modèles moléculaires</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>Structures macromoléculaires</term><term>Tryptophane (métabolisme)</term><term>Ultracentrifugation</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</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>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>Tryptophane</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Macromolecular Substances</term><term>Models, Molecular</term><term>Protein Binding</term><term>Ultracentrifugation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Facteurs de transcription</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Protéines bactériennes</term><term>Protéines de liaison à l'ARN</term><term>Structures macromoléculaires</term><term>Ultracentrifugation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The trp RNA-binding attenuation protein (TRAP) negatively regulates expression of the tryptophan biosynthesis genes of Bacillus subtilis. In the presence of tryptophan, TRAP is activated to bind to the 5'-leader region of the trp mRNA resulting in termination prior to the structural genes. In addition, accumulation of uncharged tRNA(Trp) induces synthesis of anti-TRAP (AT), which binds to TRAP and inhibits its function. Both of these proteins consist of oligomers of identical subunits. Here, we characterize the self-association of each of these proteins and the TRAP-AT interaction in free solution using equilibrium and velocity analytical ultracentrifugation. TRAP exists as a stable 11-mer in the absence and in the presence of tryptophan. Tryptophan binding induces a conformational change in TRAP. AT exists in a reversible equilibrium between trimer and dodecamer with an equilibrium constant of approximately 3 x 10(14)M(-3). About 20% of the trimer is incompetent to form dodecamer. The AT equilibrium is slow on the time-scale of the velocity experiment. Formation of TRAP-AT complexes occurs only in the presence of tryptophan. A complex containing one TRAP 11-mer and one AT 12-mer forms with high affinity. At higher ratios of TRAP:AT complexes containing two TRAP 11-mers and one AT 12-mer are detected. A model for the structure of the complex is proposed.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Connecticut</li></region></list><tree><noCountry><name sortKey="Chen, Yanling" sort="Chen, Yanling" uniqKey="Chen Y" first="Yanling" last="Chen">Yanling Chen</name><name sortKey="Cole, James L" sort="Cole, James L" uniqKey="Cole J" first="James L" last="Cole">James L. Cole</name><name sortKey="Gollnick, Paul" sort="Gollnick, Paul" uniqKey="Gollnick P" first="Paul" last="Gollnick">Paul Gollnick</name><name sortKey="Lary, Jeffrey" sort="Lary, Jeffrey" uniqKey="Lary J" first="Jeffrey" last="Lary">Jeffrey Lary</name></noCountry><country name="États-Unis"><region name="Connecticut"><name sortKey="Snyder, Doug" sort="Snyder, Doug" uniqKey="Snyder D" first="Doug" last="Snyder">Doug Snyder</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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