MersV1, PubMed, Checkpoint, bibRecord, 002623

Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.

Identifieur interne : 002623 ( PubMed/Checkpoint ); précédent : 002622; suivant : 002624

Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.

Auteurs : C. Baumann [États-Unis] ; J. Otridge ; P. Gollnick

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 1996.

RBID : pubmed:8647825

Descripteurs français

English descriptors

KwdEn :
- Bacillus subtilis (chemistry), Bacterial Proteins, Base Sequence, DNA Primers, Hydrogen-Ion Concentration, Kinetics, Molecular Sequence Data, Protein Binding, RNA, Messenger (chemistry), RNA-Binding Proteins (chemistry), RNA-Binding Proteins (genetics), RNA-Binding Proteins (metabolism), Salts, Thermodynamics, Transcription Factors (chemistry), Transcription Factors (genetics), Transcription Factors (metabolism), Tryptophan (chemistry).
MESH :
- chemical , chemistry : RNA, Messenger, RNA-Binding Proteins, Transcription Factors, Tryptophan.
- chemical , genetics : RNA-Binding Proteins, Transcription Factors.
- chemical , metabolism : RNA-Binding Proteins, Transcription Factors.
- chemical : Bacterial Proteins, DNA Primers, Salts.
- chemistry : Bacillus subtilis.
- Base Sequence, Hydrogen-Ion Concentration, Kinetics, Molecular Sequence Data, Protein Binding, Thermodynamics.

Abstract

In Bacillus subtilis, expression of the tryptophan biosynthetic genes is regulated in response to tryptophan by an RNA-binding protein called TRAP (trp RNA-binding attenuation protein). TRAP has been shown to contain 11 identical subunits arranged in a symmetrical ring. Kinetic and thermodynamic parameters of the interaction between tryptophan-activated TRAP and trp leader RNA were studied. Results from glycerol gradients and mobility shift gels indicate that two TRAP 11-mers bind to each trp leader RNA. A filter binding assay was used to determine an apparent binding constant of 8.0 +/- 1.3 x 10(9) m-1 (Kd = 0.12 +/- 0.02 nM) for TRAP and an RNA containing residues +36 to +92 of the trp leader RNA in 1 mM L-tryptophan at 37 degrees C. The temperature dependence of Kapp was somewhat unexpected demonstrating that the delta H of the interaction is highly unfavorable at + 15.9 kcal mol-1. Therefore, the interaction is completely driven by a delta S of +97 cal mol-1 K-1. The interaction between tryptophan-activated TRAP and trp leader RNA displayed broad salt and pH activity profiles. Finally, the rate of RNA dissociation from the RNA-TRAP.tryptophan ternary complex was found to be very slow in high concentrations of tryptophan (> 40 microM) but increased in lower tryptophan concentrations. This suggests that dissociation of tryptophan from the ternary complex is the rate-limiting step in RNA dissociation.

DOI: 10.1074/jbc.271.21.12269
PubMed: 8647825

Affiliations:

États-Unis

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pubmed:8647825

Le document en format XML

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<affiliation wicri:level="1"><nlm:affiliation>Department of Biological Sciences, State University of New York at Buffalo 14260, USA.</nlm:affiliation>
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<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
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<term>RNA-Binding Proteins (genetics)</term>
<term>RNA-Binding Proteins (metabolism)</term>
<term>Salts</term>
<term>Thermodynamics</term>
<term>Transcription Factors (chemistry)</term>
<term>Transcription Factors (genetics)</term>
<term>Transcription Factors (metabolism)</term>
<term>Tryptophan (chemistry)</term>
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<term>Amorces ADN</term>
<term>Bacillus subtilis ()</term>
<term>Cinétique</term>
<term>Concentration en ions d'hydrogène</term>
<term>Données de séquences moléculaires</term>
<term>Facteurs de transcription ()</term>
<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Liaison aux protéines</term>
<term>Protéines bactériennes</term>
<term>Protéines de liaison à l'ARN ()</term>
<term>Protéines de liaison à l'ARN (génétique)</term>
<term>Protéines de liaison à l'ARN (métabolisme)</term>
<term>Sels</term>
<term>Séquence nucléotidique</term>
<term>Thermodynamique</term>
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<term>RNA-Binding Proteins</term>
<term>Transcription Factors</term>
<term>Tryptophan</term>
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<term>Transcription Factors</term>
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<term>Transcription Factors</term>
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<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Thermodynamics</term>
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<keywords scheme="MESH" xml:lang="fr"><term>ARN messager</term>
<term>Amorces ADN</term>
<term>Bacillus subtilis</term>
<term>Cinétique</term>
<term>Concentration en ions d'hydrogène</term>
<term>Données de séquences moléculaires</term>
<term>Facteurs de transcription</term>
<term>Liaison aux protéines</term>
<term>Protéines bactériennes</term>
<term>Protéines de liaison à l'ARN</term>
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<term>Tryptophane</term>
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<front><div type="abstract" xml:lang="en">In Bacillus subtilis, expression of the tryptophan biosynthetic genes is regulated in response to tryptophan by an RNA-binding protein called TRAP (trp RNA-binding attenuation protein). TRAP has been shown to contain 11 identical subunits arranged in a symmetrical ring. Kinetic and thermodynamic parameters of the interaction between tryptophan-activated TRAP and trp leader RNA were studied. Results from glycerol gradients and mobility shift gels indicate that two TRAP 11-mers bind to each trp leader RNA. A filter binding assay was used to determine an apparent binding constant of 8.0 +/- 1.3 x 10(9) m-1 (Kd = 0.12 +/- 0.02 nM) for TRAP and an RNA containing residues +36 to +92 of the trp leader RNA in 1 mM L-tryptophan at 37 degrees C. The temperature dependence of Kapp was somewhat unexpected demonstrating that the delta H of the interaction is highly unfavorable at + 15.9 kcal mol-1. Therefore, the interaction is completely driven by a delta S of +97 cal mol-1 K-1. The interaction between tryptophan-activated TRAP and trp leader RNA displayed broad salt and pH activity profiles. Finally, the rate of RNA dissociation from the RNA-TRAP.tryptophan ternary complex was found to be very slow in high concentrations of tryptophan (> 40 microM) but increased in lower tryptophan concentrations. This suggests that dissociation of tryptophan from the ternary complex is the rate-limiting step in RNA dissociation.</div>
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<Abstract><AbstractText>In Bacillus subtilis, expression of the tryptophan biosynthetic genes is regulated in response to tryptophan by an RNA-binding protein called TRAP (trp RNA-binding attenuation protein). TRAP has been shown to contain 11 identical subunits arranged in a symmetrical ring. Kinetic and thermodynamic parameters of the interaction between tryptophan-activated TRAP and trp leader RNA were studied. Results from glycerol gradients and mobility shift gels indicate that two TRAP 11-mers bind to each trp leader RNA. A filter binding assay was used to determine an apparent binding constant of 8.0 +/- 1.3 x 10(9) m-1 (Kd = 0.12 +/- 0.02 nM) for TRAP and an RNA containing residues +36 to +92 of the trp leader RNA in 1 mM L-tryptophan at 37 degrees C. The temperature dependence of Kapp was somewhat unexpected demonstrating that the delta H of the interaction is highly unfavorable at + 15.9 kcal mol-1. Therefore, the interaction is completely driven by a delta S of +97 cal mol-1 K-1. The interaction between tryptophan-activated TRAP and trp leader RNA displayed broad salt and pH activity profiles. Finally, the rate of RNA dissociation from the RNA-TRAP.tryptophan ternary complex was found to be very slow in high concentrations of tryptophan (> 40 microM) but increased in lower tryptophan concentrations. This suggests that dissociation of tryptophan from the ternary complex is the rate-limiting step in RNA dissociation.</AbstractText>
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Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.

Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

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