E-Box Variants Direct Formation of Distinct Complexes with the Basic Helix-Loop-Helix Protein ALF1
Identifieur interne : 003051 ( Main/Exploration ); précédent : 003050; suivant : 003052E-Box Variants Direct Formation of Distinct Complexes with the Basic Helix-Loop-Helix Protein ALF1
Auteurs : Bjarne J. Bonven [Danemark] ; Anders L. Nielsen [Danemark] ; Peder L. N Rby [Danemark] ; Finn S. Pedersen [Danemark] ; Poul J Rgensen [Danemark]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 1995.
English descriptors
- KwdEn :
- Teeft :
- Acad, Adaptability, Alf1, Alf1 binding, Alf1 consensus site, Alf1b, Alonso cabrera, Amino, Amino acid residues, Amino acids, Amphipathic helices, Backbone, Backbone contacts, Backbone phosphate contact pattern, Backbone phosphate groups, Band intensities, Basic region, Basic regions, Bhlh, Bhlh protein, Bhlh proteins, Binding region, Binding regions, Binding site, Binding site selection, Biol, Blackwell weintraub, Bottom strand, Bottom strand results, Bovine serum albumin, Brunelle schleif, Capital letters, Cell development, Chemical interference analysis, Chevray nathans, Complete interference, Consensus sequences, Contact pattern, Contact patterns, Crystal structure, Cyc1 promoter, Depurination interference, Depyrimidation interference, Dimer, Dimeric domain, Dimethyl sulfate, Distinct complexes, Ellenberger, Ethylation, Ethylation interference, Expression vector, Fisher goding, General agreement, Helical, Helical projections, Helix, Hexameric core, Interference analysis, Interference regions, Interference results, Lacz, Lacz expression, Leucine zipper, Local conformation, Major groove, Maxam gilbert, Methylation, Methylation interference, Molecular biology, Murine, Murre, Myod, Natl, Natl acad, Nielsen, Nucleotide coordinates, Oligonucleotides, Other class, Overall extent, Partial interference, Phosphate contact pattern, Phosphate contacts, Phosphate groups, Polymerase chain reaction, Proc, Promoter, Pseudo dyad axis, Recognition mutants, Same activity, Sequence recognition, Sequence selectivity, Siebenlist gilbert, Strand, Strand results, Titration curves, Transactivating properties, Transcription, Transcription factors, Transcriptional, Transcriptional activation, Transcriptional activation domain, Unpublished results, Weintraub, Yeast.
Abstract
Abstract: The murine transcription factor ALF1 belongs to the class of basic helix-loop-helix proteins specific for the NCAGNTGN-version of the E-box. Binding of homodimeric ALF1 to variants of this motif was studied by a combination of binding site selection technology and DNA modification interference analysis. The results showed that substitutions at the non-conserved positions in the E-box sequence could cause profound alterations in the patterns of specific contacts at the protein-DNA interface. Thus, both the overall extent of the binding region and the backbone phosphate contact pattern differed markedly between closely related E-boxes with similar affinities for ALF1. The identity of the base at the inner N was an important determinant of contact pattern specification. The E-box variants differed in their ability to mediate ALF1 dependent transcriptional activationin vivo. We discuss the possibility that adaptability in basic helix-loop-helix protein-DNA interactions can result in complexes with different functional properties.
Url:
DOI: 10.1006/jmbi.1995.0319
Affiliations:
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MÕllers Allé 130, DK-8000, Aarhus C</wicri:regionArea><wicri:noRegion>Aarhus C</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="1995">1995</date><biblScope unit="volume">249</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="564">564</biblScope><biblScope unit="page" to="575">575</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>ALF1</term><term>E-box</term><term>bHLH protein</term><term>backbone contacts</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Adaptability</term><term>Alf1</term><term>Alf1 binding</term><term>Alf1 consensus site</term><term>Alf1b</term><term>Alonso cabrera</term><term>Amino</term><term>Amino acid residues</term><term>Amino acids</term><term>Amphipathic helices</term><term>Backbone</term><term>Backbone contacts</term><term>Backbone phosphate contact pattern</term><term>Backbone phosphate groups</term><term>Band intensities</term><term>Basic region</term><term>Basic regions</term><term>Bhlh</term><term>Bhlh protein</term><term>Bhlh proteins</term><term>Binding region</term><term>Binding regions</term><term>Binding site</term><term>Binding site selection</term><term>Biol</term><term>Blackwell weintraub</term><term>Bottom strand</term><term>Bottom strand results</term><term>Bovine serum albumin</term><term>Brunelle schleif</term><term>Capital letters</term><term>Cell development</term><term>Chemical interference analysis</term><term>Chevray nathans</term><term>Complete interference</term><term>Consensus sequences</term><term>Contact pattern</term><term>Contact patterns</term><term>Crystal structure</term><term>Cyc1 promoter</term><term>Depurination interference</term><term>Depyrimidation interference</term><term>Dimer</term><term>Dimeric domain</term><term>Dimethyl sulfate</term><term>Distinct complexes</term><term>Ellenberger</term><term>Ethylation</term><term>Ethylation interference</term><term>Expression vector</term><term>Fisher goding</term><term>General agreement</term><term>Helical</term><term>Helical projections</term><term>Helix</term><term>Hexameric core</term><term>Interference analysis</term><term>Interference regions</term><term>Interference results</term><term>Lacz</term><term>Lacz expression</term><term>Leucine zipper</term><term>Local conformation</term><term>Major groove</term><term>Maxam gilbert</term><term>Methylation</term><term>Methylation interference</term><term>Molecular biology</term><term>Murine</term><term>Murre</term><term>Myod</term><term>Natl</term><term>Natl acad</term><term>Nielsen</term><term>Nucleotide coordinates</term><term>Oligonucleotides</term><term>Other class</term><term>Overall extent</term><term>Partial interference</term><term>Phosphate contact pattern</term><term>Phosphate contacts</term><term>Phosphate groups</term><term>Polymerase chain reaction</term><term>Proc</term><term>Promoter</term><term>Pseudo dyad axis</term><term>Recognition mutants</term><term>Same activity</term><term>Sequence recognition</term><term>Sequence selectivity</term><term>Siebenlist gilbert</term><term>Strand</term><term>Strand results</term><term>Titration curves</term><term>Transactivating properties</term><term>Transcription</term><term>Transcription factors</term><term>Transcriptional</term><term>Transcriptional activation</term><term>Transcriptional activation domain</term><term>Unpublished results</term><term>Weintraub</term><term>Yeast</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The murine transcription factor ALF1 belongs to the class of basic helix-loop-helix proteins specific for the NCAGNTGN-version of the E-box. Binding of homodimeric ALF1 to variants of this motif was studied by a combination of binding site selection technology and DNA modification interference analysis. The results showed that substitutions at the non-conserved positions in the E-box sequence could cause profound alterations in the patterns of specific contacts at the protein-DNA interface. Thus, both the overall extent of the binding region and the backbone phosphate contact pattern differed markedly between closely related E-boxes with similar affinities for ALF1. The identity of the base at the inner N was an important determinant of contact pattern specification. The E-box variants differed in their ability to mediate ALF1 dependent transcriptional activationin vivo. We discuss the possibility that adaptability in basic helix-loop-helix protein-DNA interactions can result in complexes with different functional properties.</div></front></TEI><affiliations><list><country><li>Danemark</li></country></list><tree><country name="Danemark"><noRegion><name sortKey="Bonven, Bjarne J" sort="Bonven, Bjarne J" uniqKey="Bonven B" first="Bjarne J." last="Bonven">Bjarne J. Bonven</name></noRegion><name sortKey="J Rgensen, Poul" sort="J Rgensen, Poul" uniqKey="J Rgensen P" first="Poul" last="J Rgensen">Poul J Rgensen</name><name sortKey="N Rby, Peder L" sort="N Rby, Peder L" uniqKey="N Rby P" first="Peder L." last="N Rby">Peder L. N Rby</name><name sortKey="Nielsen, Anders L" sort="Nielsen, Anders L" uniqKey="Nielsen A" first="Anders L." last="Nielsen">Anders L. Nielsen</name><name sortKey="Pedersen, Finn S" sort="Pedersen, Finn S" uniqKey="Pedersen F" first="Finn S." last="Pedersen">Finn S. 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