The DNA Binding Domain of the Human c-Abl Tyrosine Kinase Preferentially Binds to DNA Sequences Containing an AAC Motif and to Distorted DNA Structures†
Identifieur interne : 000271 ( France/Analysis ); précédent : 000270; suivant : 000272The DNA Binding Domain of the Human c-Abl Tyrosine Kinase Preferentially Binds to DNA Sequences Containing an AAC Motif and to Distorted DNA Structures†
Auteurs : Marie-Hélène David-Cordonnier [France] ; Malika Hamdane [France, Belgique] ; Christian Bailly [France] ; Jean-Claude D'Halluin [France]Source :
- Biochemistry [ 0006-2960 ] ; 1998.
Abstract
The c-Abl tyrosine kinase protein is implicated in the signaling pathway as well as in transcription, DNA repair, apoptosis, and several other vital biological processes essential for cell proliferation or differentiation. The interaction of c-Abl with DNA is important for some of these functions, but the exact nature of this interaction is still a matter of controversy. The present study addresses the DNA-binding properties of the human c-Abl protein. Using CASTing experiments, the consensus binding site 5‘-AA/CAACAAA/C was determined. The central highly conserved AAC triplet appears to constitute the crucial core element in the binding sequences of the c-Abl protein. The c-Abl DNA-binding domain recognizes specific sequences and interacts with deformed DNA structures such as four-way junctions and bubble DNA containing a large single-stranded loop, as determined by electromobility shift assay, melting temperature studies, and binding to specific oligonucleotides covalently linked to beads. Additional competition experiments suggest that the interaction mainly involves contacts within the minor groove of the double helix. The DNA-binding properties of c-Abl are reminiscent of those of high-mobility group (HMG)-like proteins such as LEF-1 and SRY. However, the circular permutation and ring closure assays and DNA unwinding experiments reveal that, unlike HMGs, c-Abl does not bend its target sequence. In addition, it is shown that the protein potentiates the DNA relaxation activity of topoisomerase I. These findings indicate that the interaction of c-Abl with DNA is both sequence-selective and structure-dependent.
Url:
DOI: 10.1021/bi973030w
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 001294
- to stream Istex, to step Curation: 001294
- to stream Istex, to step Checkpoint: 001237
- to stream Main, to step Merge: 003A78
- to stream Main, to step Curation: 003A29
- to stream Main, to step Exploration: 003A29
- to stream France, to step Extraction: 000271
Links to Exploration step
ISTEX:F87DA1586B7DF00BF45F08DCEAEC349928DE91A6Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>The DNA Binding Domain of the Human c-Abl Tyrosine Kinase Preferentially Binds to DNA Sequences Containing an AAC Motif and to Distorted DNA Structures†</title><author><name sortKey="David Cordonnier, Marie Helene" sort="David Cordonnier, Marie Helene" uniqKey="David Cordonnier M" first="Marie-Hélène" last="David-Cordonnier">Marie-Hélène David-Cordonnier</name></author><author><name sortKey="Hamdane, Malika" sort="Hamdane, Malika" uniqKey="Hamdane M" first="Malika" last="Hamdane">Malika Hamdane</name></author><author><name sortKey="Bailly, Christian" sort="Bailly, Christian" uniqKey="Bailly C" first="Christian" last="Bailly">Christian Bailly</name></author><author><name sortKey="D Halluin, Jean Claude" sort="D Halluin, Jean Claude" uniqKey="D Halluin J" first="Jean-Claude" last="D'Halluin">Jean-Claude D'Halluin</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:F87DA1586B7DF00BF45F08DCEAEC349928DE91A6</idno><date when="1998" year="1998">1998</date><idno type="doi">10.1021/bi973030w</idno><idno type="url">https://api.istex.fr/ark:/67375/TPS-GR5T3DLS-F/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001294</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001294</idno><idno type="wicri:Area/Istex/Curation">001294</idno><idno type="wicri:Area/Istex/Checkpoint">001237</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001237</idno><idno type="wicri:doubleKey">0006-2960:1998:David Cordonnier M:the:dna:binding</idno><idno type="wicri:Area/Main/Merge">003A78</idno><idno type="wicri:Area/Main/Curation">003A29</idno><idno type="wicri:Area/Main/Exploration">003A29</idno><idno type="wicri:Area/France/Extraction">000271</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">The DNA Binding Domain of the Human c-Abl Tyrosine Kinase Preferentially
Binds to DNA Sequences Containing an AAC Motif and to Distorted DNA
Structures<ref type="bib" target="#bi973030wAF2"><hi rend="superscript">†</hi></ref></title><author><name sortKey="David Cordonnier, Marie Helene" sort="David Cordonnier, Marie Helene" uniqKey="David Cordonnier M" first="Marie-Hélène" last="David-Cordonnier">Marie-Hélène David-Cordonnier</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>INSERM U 124 Onco-hématologie Moléculaire, Institut de Recherches sur le Cancer de Lille,Place de Verdun, 59045 Lille, France, and Centre Oscar Lambret, Place de Verdun, 59045 Lille</wicri:regionArea><placeName><region type="region" nuts="2">Hauts-de-France</region><region type="old region" nuts="2">Nord-Pas-de-Calais</region><settlement type="city">Lille</settlement></placeName></affiliation><affiliation></affiliation></author><author><name sortKey="Hamdane, Malika" sort="Hamdane, Malika" uniqKey="Hamdane M" first="Malika" last="Hamdane">Malika Hamdane</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>INSERM U 124 Onco-hématologie Moléculaire, Institut de Recherches sur le Cancer de Lille,Place de Verdun, 59045 Lille, France, and Centre Oscar Lambret, Place de Verdun, 59045 Lille</wicri:regionArea><placeName><region type="region" nuts="2">Hauts-de-France</region><region type="old region" nuts="2">Nord-Pas-de-Calais</region><settlement type="city">Lille</settlement></placeName></affiliation><affiliation></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Belgique</country><wicri:regionArea> Present address: IRIBHN, Erasme Hospital,U.L.B., 808 Routede Lennik, B-1070 Brussels</wicri:regionArea><wicri:noRegion>B-1070 Brussels</wicri:noRegion></affiliation></author><author><name sortKey="Bailly, Christian" sort="Bailly, Christian" uniqKey="Bailly C" first="Christian" last="Bailly">Christian Bailly</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>INSERM U 124 Onco-hématologie Moléculaire, Institut de Recherches sur le Cancer de Lille,Place de Verdun, 59045 Lille, France, and Centre Oscar Lambret, Place de Verdun, 59045 Lille</wicri:regionArea><placeName><region type="region" nuts="2">Hauts-de-France</region><region type="old region" nuts="2">Nord-Pas-de-Calais</region><settlement type="city">Lille</settlement></placeName></affiliation><affiliation></affiliation><affiliation></affiliation></author><author><name sortKey="D Halluin, Jean Claude" sort="D Halluin, Jean Claude" uniqKey="D Halluin J" first="Jean-Claude" last="D'Halluin">Jean-Claude D'Halluin</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>INSERM U 124 Onco-hématologie Moléculaire, Institut de Recherches sur le Cancer de Lille,Place de Verdun, 59045 Lille, France, and Centre Oscar Lambret, Place de Verdun, 59045 Lille</wicri:regionArea><placeName><region type="region" nuts="2">Hauts-de-France</region><region type="old region" nuts="2">Nord-Pas-de-Calais</region><settlement type="city">Lille</settlement></placeName></affiliation><affiliation></affiliation><affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Biochemistry</title><title level="j" type="abbrev">Biochemistry</title><idno type="ISSN">0006-2960</idno><idno type="eISSN">1520-4995</idno><imprint><publisher>American Chemical Society</publisher><date type="e-published">1998</date><date type="published">1998</date><biblScope unit="vol">37</biblScope><biblScope unit="issue">17</biblScope><biblScope unit="page" from="6065">6065</biblScope><biblScope unit="page" to="6076">6076</biblScope></imprint><idno type="ISSN">0006-2960</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-2960</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">The c-Abl tyrosine kinase protein is implicated in the signaling pathway as well as in transcription, DNA repair, apoptosis, and several other vital biological processes essential for cell proliferation or differentiation. The interaction of c-Abl with DNA is important for some of these functions, but the exact nature of this interaction is still a matter of controversy. The present study addresses the DNA-binding properties of the human c-Abl protein. Using CASTing experiments, the consensus binding site 5‘-AA/CAACAAA/C was determined. The central highly conserved AAC triplet appears to constitute the crucial core element in the binding sequences of the c-Abl protein. The c-Abl DNA-binding domain recognizes specific sequences and interacts with deformed DNA structures such as four-way junctions and bubble DNA containing a large single-stranded loop, as determined by electromobility shift assay, melting temperature studies, and binding to specific oligonucleotides covalently linked to beads. Additional competition experiments suggest that the interaction mainly involves contacts within the minor groove of the double helix. The DNA-binding properties of c-Abl are reminiscent of those of high-mobility group (HMG)-like proteins such as LEF-1 and SRY. However, the circular permutation and ring closure assays and DNA unwinding experiments reveal that, unlike HMGs, c-Abl does not bend its target sequence. In addition, it is shown that the protein potentiates the DNA relaxation activity of topoisomerase I. These findings indicate that the interaction of c-Abl with DNA is both sequence-selective and structure-dependent.</div></front></TEI><affiliations><list><country><li>Belgique</li><li>France</li></country><region><li>Hauts-de-France</li><li>Nord-Pas-de-Calais</li></region><settlement><li>Lille</li></settlement></list><tree><country name="France"><region name="Hauts-de-France"><name sortKey="David Cordonnier, Marie Helene" sort="David Cordonnier, Marie Helene" uniqKey="David Cordonnier M" first="Marie-Hélène" last="David-Cordonnier">Marie-Hélène David-Cordonnier</name></region><name sortKey="Bailly, Christian" sort="Bailly, Christian" uniqKey="Bailly C" first="Christian" last="Bailly">Christian Bailly</name><name sortKey="D Halluin, Jean Claude" sort="D Halluin, Jean Claude" uniqKey="D Halluin J" first="Jean-Claude" last="D'Halluin">Jean-Claude D'Halluin</name><name sortKey="Hamdane, Malika" sort="Hamdane, Malika" uniqKey="Hamdane M" first="Malika" last="Hamdane">Malika Hamdane</name></country><country name="Belgique"><noRegion><name sortKey="Hamdane, Malika" sort="Hamdane, Malika" uniqKey="Hamdane M" first="Malika" last="Hamdane">Malika Hamdane</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/France/Analysis
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000271 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/France/Analysis/biblio.hfd -nk 000271 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= France
|étape= Analysis
|type= RBID
|clé= ISTEX:F87DA1586B7DF00BF45F08DCEAEC349928DE91A6
|texte= The DNA Binding Domain of the Human c-Abl Tyrosine Kinase Preferentially Binds to DNA Sequences Containing an AAC Motif and to Distorted DNA Structures†
}}
| This area was generated with Dilib version V0.6.33. |  |