Characterization of a trp RNA-binding attenuation protein (TRAP) mutant with tryptophan independent RNA binding activity.
Identifieur interne : 003077 ( Main/Exploration ); précédent : 003076; suivant : 003078Characterization of a trp RNA-binding attenuation protein (TRAP) mutant with tryptophan independent RNA binding activity.
Auteurs : Pan T X. Li [États-Unis] ; Paul GollnickSource :
- Journal of molecular biology [ 0022-2836 ] ; 2004.
Descripteurs français
- KwdFr :
- ARN (métabolisme), Bacillus subtilis (), Concentration osmolaire, Conformation des protéines, Facteurs de transcription (), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Liaison aux protéines (génétique), Ligands, Mutation faux-sens, Protéines bactériennes (), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Protéines de liaison à l'ARN (), Protéines de liaison à l'ARN (génétique), Protéines de liaison à l'ARN (métabolisme), Sous-unités de protéines (génétique), Tryptophane (analogues et dérivés), Tryptophane (métabolisme).
- MESH :
- analogues et dérivés : Tryptophane.
- génétique : Facteurs de transcription, Liaison aux protéines, Protéines bactériennes, Protéines de liaison à l'ARN, Sous-unités de protéines.
- métabolisme : ARN, Facteurs de transcription, Protéines bactériennes, Protéines de liaison à l'ARN, Tryptophane.
- Bacillus subtilis, Concentration osmolaire, Conformation des protéines, Facteurs de transcription, Ligands, Mutation faux-sens, Protéines bactériennes, Protéines de liaison à l'ARN.
English descriptors
- KwdEn :
- Bacillus subtilis (chemistry), Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Ligands, Mutation, Missense, Osmolar Concentration, Protein Binding (genetics), Protein Conformation, Protein Subunits (genetics), RNA (metabolism), RNA-Binding Proteins (chemistry), RNA-Binding Proteins (genetics), RNA-Binding Proteins (metabolism), Transcription Factors (chemistry), Transcription Factors (genetics), Transcription Factors (metabolism), Tryptophan (analogs & derivatives), Tryptophan (metabolism).
- MESH :
- chemical , analogs & derivatives : Tryptophan.
- chemical , chemistry : Bacterial Proteins, RNA-Binding Proteins, Transcription Factors.
- chemistry : Bacillus subtilis.
- chemical , genetics : Bacterial Proteins, Protein Binding, Protein Subunits, RNA-Binding Proteins, Transcription Factors.
- chemical , metabolism : Bacterial Proteins, RNA, RNA-Binding Proteins, Transcription Factors, Tryptophan.
- chemical : Ligands, Mutation, Missense, Osmolar Concentration, Protein Conformation.
Abstract
TRAP (trp RNA-binding attenuation protein) is an 11 subunit RNA-binding protein that regulates expression of genes involved in tryptophan metabolism (trp) in Bacillus subtilis in response to changes in intracellular tryptophan concentration. When activated by binding up to 11 tryptophan residues, TRAP binds to the mRNAs of several trp genes and down-regulates their expression. Recently, a TRAP mutant was found that binds RNA in the absence of tryptophan. In this mutant protein, Thr30, which is part of the tryptophan-binding site, is replaced with Val (T30V). We have compared the RNA-binding properties of T30V and wild-type (WT) TRAP, as well as of a series of hetero-11-mers containing mixtures of WT and T30V TRAP subunits. The most significant difference between the interaction of T30V and WT TRAP with RNA is that the affinity of T30V TRAP is more dependent on ionic strength. Analysis of the hetero-11-mers allowed us to examine how subunits interact within an 11-mer with regard to binding to tryptophan or RNA. Our data suggest that individual subunits retain properties similar to those observed when they are in homo-11-mers and that individual G/UAG triplets within the RNA can bind to TRAP differently.
DOI: 10.1016/j.jmb.2003.11.002
PubMed: 14687568
Affiliations:
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Le document en format XML
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<term>Ligands</term>
<term>Mutation, Missense</term>
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<term>Protein Conformation</term>
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<term>Bacillus subtilis ()</term>
<term>Concentration osmolaire</term>
<term>Conformation des protéines</term>
<term>Facteurs de transcription ()</term>
<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Liaison aux protéines (génétique)</term>
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<term>Protéines bactériennes (génétique)</term>
<term>Protéines bactériennes (métabolisme)</term>
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<term>Protéines de liaison à l'ARN (métabolisme)</term>
<term>Sous-unités de protéines (génétique)</term>
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<term>Sous-unités de protéines</term>
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<term>Conformation des protéines</term>
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<front><div type="abstract" xml:lang="en">TRAP (trp RNA-binding attenuation protein) is an 11 subunit RNA-binding protein that regulates expression of genes involved in tryptophan metabolism (trp) in Bacillus subtilis in response to changes in intracellular tryptophan concentration. When activated by binding up to 11 tryptophan residues, TRAP binds to the mRNAs of several trp genes and down-regulates their expression. Recently, a TRAP mutant was found that binds RNA in the absence of tryptophan. In this mutant protein, Thr30, which is part of the tryptophan-binding site, is replaced with Val (T30V). We have compared the RNA-binding properties of T30V and wild-type (WT) TRAP, as well as of a series of hetero-11-mers containing mixtures of WT and T30V TRAP subunits. The most significant difference between the interaction of T30V and WT TRAP with RNA is that the affinity of T30V TRAP is more dependent on ionic strength. Analysis of the hetero-11-mers allowed us to examine how subunits interact within an 11-mer with regard to binding to tryptophan or RNA. Our data suggest that individual subunits retain properties similar to those observed when they are in homo-11-mers and that individual G/UAG triplets within the RNA can bind to TRAP differently.</div>
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