Interaction of the trp RNA-binding attenuation protein (TRAP) with anti-TRAP.
Identifieur interne : 000276 ( Ncbi/Merge ); précédent : 000275; suivant : 000277Interaction 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
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pubmed:15099736Le document en format XML
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<wicri:regionArea>Department of Molecular and Cell Biology, University of Connecticut, 91 N. Eagleville Road, U-3125, Storrs, CT 06269</wicri:regionArea>
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<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>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Bacillus subtilis (métabolisme)</term>
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<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
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<term>Protéines de liaison à l'ARN ()</term>
<term>Protéines de liaison à l'ARN (métabolisme)</term>
<term>Structures macromoléculaires</term>
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<term>Ultracentrifugation</term>
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<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Protéines bactériennes</term>
<term>Protéines de liaison à l'ARN</term>
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<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>
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<Abstract><AbstractText>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.</AbstractText>
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