Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.
Identifieur interne : 002774 ( PubMed/Corpus ); précédent : 002773; suivant : 002775Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.
Auteurs : C. Baumann ; J. Otridge ; P. GollnickSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1996.
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
Links to Exploration step
pubmed:8647825Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.</title>
<author><name sortKey="Baumann, C" sort="Baumann, C" uniqKey="Baumann C" first="C" last="Baumann">C. Baumann</name>
<affiliation><nlm:affiliation>Department of Biological Sciences, State University of New York at Buffalo 14260, USA.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Otridge, J" sort="Otridge, J" uniqKey="Otridge J" first="J" last="Otridge">J. Otridge</name>
</author>
<author><name sortKey="Gollnick, P" sort="Gollnick, P" uniqKey="Gollnick P" first="P" last="Gollnick">P. Gollnick</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="1996">1996</date>
<idno type="RBID">pubmed:8647825</idno>
<idno type="pmid">8647825</idno>
<idno type="doi">10.1074/jbc.271.21.12269</idno>
<idno type="wicri:Area/PubMed/Corpus">002774</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002774</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.</title>
<author><name sortKey="Baumann, C" sort="Baumann, C" uniqKey="Baumann C" first="C" last="Baumann">C. Baumann</name>
<affiliation><nlm:affiliation>Department of Biological Sciences, State University of New York at Buffalo 14260, USA.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Otridge, J" sort="Otridge, J" uniqKey="Otridge J" first="J" last="Otridge">J. Otridge</name>
</author>
<author><name sortKey="Gollnick, P" sort="Gollnick, P" uniqKey="Gollnick P" first="P" last="Gollnick">P. Gollnick</name>
</author>
</analytic>
<series><title level="j">The Journal of biological chemistry</title>
<idno type="ISSN">0021-9258</idno>
<imprint><date when="1996" type="published">1996</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacillus subtilis (chemistry)</term>
<term>Bacterial Proteins</term>
<term>Base Sequence</term>
<term>DNA Primers</term>
<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>RNA, Messenger (chemistry)</term>
<term>RNA-Binding Proteins (chemistry)</term>
<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>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>RNA, Messenger</term>
<term>RNA-Binding Proteins</term>
<term>Transcription Factors</term>
<term>Tryptophan</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>RNA-Binding Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>RNA-Binding Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Bacterial Proteins</term>
<term>DNA Primers</term>
<term>Salts</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Bacillus subtilis</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term>
<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Thermodynamics</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<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>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8647825</PMID>
<DateCompleted><Year>1996</Year>
<Month>07</Month>
<Day>22</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>05</Month>
<Day>08</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN>
<JournalIssue CitedMedium="Print"><Volume>271</Volume>
<Issue>21</Issue>
<PubDate><Year>1996</Year>
<Month>May</Month>
<Day>24</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation>
</Journal>
<ArticleTitle>Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.</ArticleTitle>
<Pagination><MedlinePgn>12269-74</MedlinePgn>
</Pagination>
<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>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Baumann</LastName>
<ForeName>C</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Department of Biological Sciences, State University of New York at Buffalo 14260, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Otridge</LastName>
<ForeName>J</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Gollnick</LastName>
<ForeName>P</ForeName>
<Initials>P</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Biol Chem</MedlineTA>
<NlmUniqueID>2985121R</NlmUniqueID>
<ISSNLinking>0021-9258</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C079092">MtrB protein, Bacteria</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D016601">RNA-Binding Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D012492">Salts</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber>
<NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D001412" MajorTopicYN="N">Bacillus subtilis</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001426" MajorTopicYN="Y">Bacterial Proteins</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012333" MajorTopicYN="N">RNA, Messenger</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016601" MajorTopicYN="N">RNA-Binding Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012492" MajorTopicYN="N">Salts</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year>
<Month>5</Month>
<Day>24</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>1996</Year>
<Month>5</Month>
<Day>24</Day>
<Hour>0</Hour>
<Minute>1</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>1996</Year>
<Month>5</Month>
<Day>24</Day>
<Hour>0</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">8647825</ArticleId>
<ArticleId IdType="doi">10.1074/jbc.271.21.12269</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002774 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 002774 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= MersV1 |flux= PubMed |étape= Corpus |type= RBID |clé= pubmed:8647825 |texte= Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:8647825" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \ | NlmPubMed2Wicri -a MersV1
This area was generated with Dilib version V0.6.33. |