High-affinity DNA binding by the C-terminal domain of the transcriptional coactivator PC4 requires simultaneous interaction with two opposing unpaired strands and results in helix destabilization
Identifieur interne : 003B62 ( Main/Exploration ); précédent : 003B61; suivant : 003B63High-affinity DNA binding by the C-terminal domain of the transcriptional coactivator PC4 requires simultaneous interaction with two opposing unpaired strands and results in helix destabilization
Auteurs : Sebastiaan Werten [Pays-Bas] ; Friso W. M Langen [Pays-Bas] ; Richard Van Schaik [Pays-Bas] ; H. Th. Marc Timmers [Pays-Bas] ; Michael Meisterernst [Allemagne] ; Peter C. Van Der Vliet [Pays-Bas]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 1998.
English descriptors
- KwdEn :
- Teeft :
- Academic press, Activator, Adml promoter, Assay, Basal, Basal factors, Binding, Binding assays, Binding curves, Binding mode, Binding model, Binding protein, Binding reaction, Binding reactions, Biol, Clear function, Cofactor, Crystal structure, Dnase, Domain, Duplex, Duplex regions, Equilibrium dissociation, Footprinting analysis, Full unwinding, General transcriptional cofactor, Helix destabilization, Heteroduplex, Heteroduplex region, Heteroduplex saturation, High protein concentrations, Imagequant software, Intact protein, Kretzschmar, Langmuir isotherm, Large subunit, Larger part, Lower panel, Mismatch, Mobility shift, Molecular dynamics, Nucleotide, Oligonucleotide, Oligonucleotide heteroduplex, Oligonucleotides, Opposite directions, Pc4ctd, Pc4ctd binding, Promoter, Promoter opening, Protein concentrations, Protein particle, Replication, Replication protein, Roeder, Simultaneous interaction, Single strands, Ssdna, Ssdna binding, Ssdna binding properties, Such structures, Terminus, Transcription, Transcription factor, Transcription initiation, Transcriptional, Transcriptional activation, Transcriptional activators, Transcriptional coactivator, Trends biol, Unpublished results, Unwinding, Unwinding activity, Unwinding assays, Unwound duplex structures, Upper panel.
Abstract
Abstract: The general transcriptional cofactor PC4 enhances transcription from various promoters and functions with a wide range of transcriptional activators. Earlier studies have suggested that this enhancement originates mostly from stabilization of the TATA-box/TFIID/TFIIA complex by simultaneous interaction of PC4 with transactivation domains of upstream-binding factors and the basal factor TFIIA. However, the C-terminal half of the protein also has been shown to exhibit substantial ssDNA binding properties, to which as yet no clear function has been assigned. We have investigated the interaction of this domain with various DNA structures and report that high-affinity binding, characterized by an equilibrium dissociation constant in the nanomolar range, requires either a heteroduplex containing a minimum of about eight mismatches, or alternatively a single-stranded DNA molecule consisting of 16 to 20 nucleotides. Furthermore, both juxtaposed single strands of a heteroduplex are protected by the C-terminal domain of PC4 in DNase I footprinting experiments, whereas the double-stranded regions do not appear to be contacted. We conclude from these observations that the role of PC4 ssDNA binding is likely to involve simultaneous interaction with opposing strands in internally melted duplexes, or the induction of a pronounced distortion in the local structure of ssDNA that results in a similar juxtaposed arrangement of single strands. In addition, we have observed that both the PC4 C-terminal domain and the intact PC4 destabilize dsDNA and we discuss the possible involvement of PC4 in promoter opening and other strand displacement events.
Url:
DOI: 10.1006/jmbi.1997.1534
Affiliations:
- Allemagne, Pays-Bas
- Bavière, District de Haute-Bavière
- Munich
- Université Louis-et-Maximilien de Munich
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M" last="Langen">Friso W. M Langen</name><affiliation wicri:level="1"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratorium voor Fysiologische Chemie Universiteit Utrecht Stratenum, Universiteitsweg 100</wicri:regionArea><wicri:noRegion>Universiteitsweg 100</wicri:noRegion></affiliation></author><author><name sortKey="Van Schaik, Richard" sort="Van Schaik, Richard" uniqKey="Van Schaik R" first="Richard" last="Van Schaik">Richard Van Schaik</name><affiliation wicri:level="1"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratorium voor Fysiologische Chemie Universiteit Utrecht Stratenum, Universiteitsweg 100</wicri:regionArea><wicri:noRegion>Universiteitsweg 100</wicri:noRegion></affiliation></author><author><name sortKey="Timmers, H Th Marc" sort="Timmers, H Th Marc" uniqKey="Timmers H" first="H. Th. Marc" last="Timmers">H. Th. Marc Timmers</name><affiliation wicri:level="1"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratorium voor Fysiologische Chemie Universiteit Utrecht Stratenum, Universiteitsweg 100</wicri:regionArea><wicri:noRegion>Universiteitsweg 100</wicri:noRegion></affiliation></author><author><name sortKey="Meisterernst, Michael" sort="Meisterernst, Michael" uniqKey="Meisterernst M" first="Michael" last="Meisterernst">Michael Meisterernst</name><affiliation wicri:level="4"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Laboratorium für Molekulare Biologie, Genzentrum der Ludwig-Maximilians-Universität München, Feodor-Lynen-Straße 25 81377 München</wicri:regionArea><placeName><region type="land" nuts="1">Bavière</region><region type="district" nuts="2">District de Haute-Bavière</region><settlement type="city">Munich</settlement></placeName><orgName type="university">Université Louis-et-Maximilien de Munich</orgName></affiliation></author><author><name sortKey="Van Der Vliet, Peter C" sort="Van Der Vliet, Peter C" uniqKey="Van Der Vliet P" first="Peter C" last="Van Der Vliet">Peter C. Van Der Vliet</name><affiliation wicri:level="1"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Laboratorium voor Fysiologische Chemie Universiteit Utrecht Stratenum, Universiteitsweg 100</wicri:regionArea><wicri:noRegion>Universiteitsweg 100</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="ISSN">0022-2836</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998">1998</date><biblScope unit="volume">276</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="367">367</biblScope><biblScope unit="page" to="377">377</biblScope></imprint><idno type="ISSN">0022-2836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-2836</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adml promoter</term><term>DNA unwinding</term><term>EMSA</term><term>NC</term><term>PC</term><term>TAD</term><term>TAF</term><term>TBP</term><term>TFII</term><term>ds</term><term>heteroduplex</term><term>protein-DNA interaction</term><term>ss</term><term>ssDNA binding</term><term>transcriptional cofactor</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Activator</term><term>Adml promoter</term><term>Assay</term><term>Basal</term><term>Basal factors</term><term>Binding</term><term>Binding assays</term><term>Binding curves</term><term>Binding mode</term><term>Binding model</term><term>Binding protein</term><term>Binding reaction</term><term>Binding reactions</term><term>Biol</term><term>Clear function</term><term>Cofactor</term><term>Crystal structure</term><term>Dnase</term><term>Domain</term><term>Duplex</term><term>Duplex regions</term><term>Equilibrium dissociation</term><term>Footprinting analysis</term><term>Full unwinding</term><term>General transcriptional cofactor</term><term>Helix destabilization</term><term>Heteroduplex</term><term>Heteroduplex region</term><term>Heteroduplex saturation</term><term>High protein concentrations</term><term>Imagequant software</term><term>Intact protein</term><term>Kretzschmar</term><term>Langmuir isotherm</term><term>Large subunit</term><term>Larger part</term><term>Lower panel</term><term>Mismatch</term><term>Mobility shift</term><term>Molecular dynamics</term><term>Nucleotide</term><term>Oligonucleotide</term><term>Oligonucleotide heteroduplex</term><term>Oligonucleotides</term><term>Opposite directions</term><term>Pc4ctd</term><term>Pc4ctd binding</term><term>Promoter</term><term>Promoter opening</term><term>Protein concentrations</term><term>Protein particle</term><term>Replication</term><term>Replication protein</term><term>Roeder</term><term>Simultaneous interaction</term><term>Single strands</term><term>Ssdna</term><term>Ssdna binding</term><term>Ssdna binding properties</term><term>Such structures</term><term>Terminus</term><term>Transcription</term><term>Transcription factor</term><term>Transcription initiation</term><term>Transcriptional</term><term>Transcriptional activation</term><term>Transcriptional activators</term><term>Transcriptional coactivator</term><term>Trends biol</term><term>Unpublished results</term><term>Unwinding</term><term>Unwinding activity</term><term>Unwinding assays</term><term>Unwound duplex structures</term><term>Upper panel</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The general transcriptional cofactor PC4 enhances transcription from various promoters and functions with a wide range of transcriptional activators. Earlier studies have suggested that this enhancement originates mostly from stabilization of the TATA-box/TFIID/TFIIA complex by simultaneous interaction of PC4 with transactivation domains of upstream-binding factors and the basal factor TFIIA. However, the C-terminal half of the protein also has been shown to exhibit substantial ssDNA binding properties, to which as yet no clear function has been assigned. We have investigated the interaction of this domain with various DNA structures and report that high-affinity binding, characterized by an equilibrium dissociation constant in the nanomolar range, requires either a heteroduplex containing a minimum of about eight mismatches, or alternatively a single-stranded DNA molecule consisting of 16 to 20 nucleotides. Furthermore, both juxtaposed single strands of a heteroduplex are protected by the C-terminal domain of PC4 in DNase I footprinting experiments, whereas the double-stranded regions do not appear to be contacted. We conclude from these observations that the role of PC4 ssDNA binding is likely to involve simultaneous interaction with opposing strands in internally melted duplexes, or the induction of a pronounced distortion in the local structure of ssDNA that results in a similar juxtaposed arrangement of single strands. In addition, we have observed that both the PC4 C-terminal domain and the intact PC4 destabilize dsDNA and we discuss the possible involvement of PC4 in promoter opening and other strand displacement events.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Pays-Bas</li></country><region><li>Bavière</li><li>District de Haute-Bavière</li></region><settlement><li>Munich</li></settlement><orgName><li>Université Louis-et-Maximilien de Munich</li></orgName></list><tree><country name="Pays-Bas"><noRegion><name sortKey="Werten, Sebastiaan" sort="Werten, Sebastiaan" uniqKey="Werten S" first="Sebastiaan" last="Werten">Sebastiaan Werten</name></noRegion><name sortKey="Langen, Friso W M" sort="Langen, Friso W M" uniqKey="Langen F" first="Friso W. M" last="Langen">Friso W. M Langen</name><name sortKey="Timmers, H Th Marc" sort="Timmers, H Th Marc" uniqKey="Timmers H" first="H. Th. Marc" last="Timmers">H. Th. Marc Timmers</name><name sortKey="Van Der Vliet, Peter C" sort="Van Der Vliet, Peter C" uniqKey="Van Der Vliet P" first="Peter C" last="Van Der Vliet">Peter C. Van Der Vliet</name><name sortKey="Van Schaik, Richard" sort="Van Schaik, Richard" uniqKey="Van Schaik R" first="Richard" last="Van Schaik">Richard Van Schaik</name></country><country name="Allemagne"><region name="Bavière"><name sortKey="Meisterernst, Michael" sort="Meisterernst, Michael" uniqKey="Meisterernst M" first="Michael" last="Meisterernst">Michael Meisterernst</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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