Fos-Jun heterodimers and jun homodimers bend DNA in opposite orientations: Implications for transcription factor cooperativity
Identifieur interne : 004936 ( Main/Exploration ); précédent : 004935; suivant : 004937Fos-Jun heterodimers and jun homodimers bend DNA in opposite orientations: Implications for transcription factor cooperativity
Auteurs : Tom K. Kerppola [États-Unis] ; Tom Curran [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1991.
English descriptors
- Teeft :
- Additional regions, Amino acid residues, Analysis probes, Average mobility, Base pairs, Bends, Binding site, Binding sites, Biol, Circular permutation analysis, Circular permutation function, Circularly permuted probes, Complex mobilities, Conformational change, Cosine function, Crothers, Crystal structure, Curran, Different experiments, Different positions, Dimerization, Dnabinding domains, Electrophoretic, Electrophoretic mobilities, Electrophoretic mobility shift analysis, Flexure, Flexure angles, Fosjun heterodimers, Free probes, Gene regulation, Glucocorticoid receptor, Helix, Helix trajectories, Heterodimer, Heterodimers, Homodimer, Homodimer complexes, Homodimers, Identical lengths, Identical results, Independent experiments, Integration host factor, Intrinsic, Intrinsic bends, Landy, Leucine, Leucine region, Leucine region peptides, Leucine region proteins, Leucine zipper, Major groove, Minor groove, Mobility, Mobility patterns, Mobility variations, Moitoso, Molecular models, Nickel chelate affinity chromatography, Nitrogen fixation operons, Opposite orientations, Other peptides, Peptide, Permutation, Permutation analysis, Plasmid, Polyacrylamide, Probe, Probe mobilities, Prolactin gene, Protein complexes, Regulatory elements, Relative mobilities, Same orientations, Same sequences, Second molecule, Spacer, Spacer length, Spacer lengths, Standard deviation, Standard deviations, Structural distortion, Transcription, Transcription activation, Transcription factor, Transcription factors, Transcription initiation, Transcription regulation, Transcriptional, Transcriptional activator, Transcriptional activity, Unpublished data, Vargas, Xylene cyanol, Zipper.
Abstract
Abstract: Association of Fos and Jun with the AP-1 site results in a conformational change in the basic amino acid regions that constitute the DNA-binding domain. We show that Fos and Jun induce a corresponding alteration in the conformation of the DNA helix. Circular permutation analysis indicated that both Fos-Jun heterodimers and Jun homodimers induce flexure at the AP-1 site. Phasing analysis demonstrated that Fos-Jun heterodimers and Jun homodimers induce DNA bends that are directed in opposite orientations. Fos-Jun heterodimers bend DNA toward the major groove, whereas Jun homodimers bend DNA toward the minor groove. Fos and Jun peptides encompassing the dimerization and DNA-binding domains bend DNA in the same orientations as the full-length proteins. However, additional regions of both proteins influence the magnitude of the DNA bend angle. Thus, despite the amino acid sequence similarity in the basic region Fos-Jun heterodimers and Jun homodimers form topologically distinct DNA-protein complexes.
Url:
DOI: 10.1016/0092-8674(91)90621-5
Affiliations:
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Kerppola</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Oncology and Virology Roche Institute of Molecular Biology Nutley, New Jersey 07110</wicri:regionArea><wicri:noRegion>New Jersey 07110</wicri:noRegion></affiliation></author><author><name sortKey="Curran, Tom" sort="Curran, Tom" uniqKey="Curran T" first="Tom" last="Curran">Tom Curran</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Oncology and Virology Roche Institute of Molecular Biology Nutley, New Jersey 07110</wicri:regionArea><wicri:noRegion>New Jersey 07110</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991">1991</date><biblScope unit="volume">66</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="317">317</biblScope><biblScope unit="page" to="326">326</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Additional regions</term><term>Amino acid residues</term><term>Analysis probes</term><term>Average mobility</term><term>Base pairs</term><term>Bends</term><term>Binding site</term><term>Binding sites</term><term>Biol</term><term>Circular permutation analysis</term><term>Circular permutation function</term><term>Circularly permuted probes</term><term>Complex mobilities</term><term>Conformational change</term><term>Cosine function</term><term>Crothers</term><term>Crystal structure</term><term>Curran</term><term>Different experiments</term><term>Different positions</term><term>Dimerization</term><term>Dnabinding domains</term><term>Electrophoretic</term><term>Electrophoretic mobilities</term><term>Electrophoretic mobility shift analysis</term><term>Flexure</term><term>Flexure angles</term><term>Fosjun heterodimers</term><term>Free probes</term><term>Gene regulation</term><term>Glucocorticoid receptor</term><term>Helix</term><term>Helix trajectories</term><term>Heterodimer</term><term>Heterodimers</term><term>Homodimer</term><term>Homodimer complexes</term><term>Homodimers</term><term>Identical lengths</term><term>Identical results</term><term>Independent experiments</term><term>Integration host factor</term><term>Intrinsic</term><term>Intrinsic bends</term><term>Landy</term><term>Leucine</term><term>Leucine region</term><term>Leucine region peptides</term><term>Leucine region proteins</term><term>Leucine zipper</term><term>Major groove</term><term>Minor groove</term><term>Mobility</term><term>Mobility patterns</term><term>Mobility variations</term><term>Moitoso</term><term>Molecular models</term><term>Nickel chelate affinity chromatography</term><term>Nitrogen fixation operons</term><term>Opposite orientations</term><term>Other peptides</term><term>Peptide</term><term>Permutation</term><term>Permutation analysis</term><term>Plasmid</term><term>Polyacrylamide</term><term>Probe</term><term>Probe mobilities</term><term>Prolactin gene</term><term>Protein complexes</term><term>Regulatory elements</term><term>Relative mobilities</term><term>Same orientations</term><term>Same sequences</term><term>Second molecule</term><term>Spacer</term><term>Spacer length</term><term>Spacer lengths</term><term>Standard deviation</term><term>Standard deviations</term><term>Structural distortion</term><term>Transcription</term><term>Transcription activation</term><term>Transcription factor</term><term>Transcription factors</term><term>Transcription initiation</term><term>Transcription regulation</term><term>Transcriptional</term><term>Transcriptional activator</term><term>Transcriptional activity</term><term>Unpublished data</term><term>Vargas</term><term>Xylene cyanol</term><term>Zipper</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Association of Fos and Jun with the AP-1 site results in a conformational change in the basic amino acid regions that constitute the DNA-binding domain. We show that Fos and Jun induce a corresponding alteration in the conformation of the DNA helix. Circular permutation analysis indicated that both Fos-Jun heterodimers and Jun homodimers induce flexure at the AP-1 site. Phasing analysis demonstrated that Fos-Jun heterodimers and Jun homodimers induce DNA bends that are directed in opposite orientations. Fos-Jun heterodimers bend DNA toward the major groove, whereas Jun homodimers bend DNA toward the minor groove. Fos and Jun peptides encompassing the dimerization and DNA-binding domains bend DNA in the same orientations as the full-length proteins. However, additional regions of both proteins influence the magnitude of the DNA bend angle. Thus, despite the amino acid sequence similarity in the basic region Fos-Jun heterodimers and Jun homodimers form topologically distinct DNA-protein complexes.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Kerppola, Tom K" sort="Kerppola, Tom K" uniqKey="Kerppola T" first="Tom K." last="Kerppola">Tom K. Kerppola</name></noRegion><name sortKey="Curran, Tom" sort="Curran, Tom" uniqKey="Curran T" first="Tom" last="Curran">Tom Curran</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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