Source:http://linkedlifedata.com/resource/pubmed/id/17705400
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
36
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pubmed:dateCreated |
2007-9-4
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pubmed:abstractText |
Myc and Max belong to the b-HLH-LZ family of transcription factors. Heterodimerization between Myc and Max or homodimerization of Max allows these proteins to bind their cognate DNA sequence known as the E-box (CACGTG). Recent evidence has suggested that the c-Myc/Max heterodimeric b-HLH-LZ could interact to form a head-to-tail dimer of dimers and induce complex topologies such as loops in promoters containing more than one E-box sequence. In an attempt to shed light on this hypothesis, the interaction between the heterodimeric b-HLH-LZ of c-Myc/Max and a fragment of the hTERT promoter containing two E-box sequences was studied by atomic force microscopy. Specific binding events were observed at both E-box sites with equal probabilities. In accordance with previous results obtained by EMSA, we observed that the specific binding of the c-Myc/Max b-HLH-LZ bends the promoter. However no looping could be observed in a wide range of concentration encompassing the Ka (association constant) of the putative tetramer and the Ka for the specific binding of the heterodimer. In contrast, experiments performed with a mandatory c-Myc/Max b-HLH-LZ tetramer incubated with the hTERT promoter fragment allowed for the visualization of loops and cross-linked DNA strands originating from specific binding. Altogether, our results indicate that the c-Myc/Max b-HLH-LZ dimer binds specifically and equally to both E-box sites of the hTERT promoter and induces a significant bending of the promoter and that the suggested oligomerization of the c-Myc/Max heterodimeric b-HLH-LZ, if existing, is most likely too weak to induce the formation of a loop in a promoter.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Basic-Leucine Zipper Transcription...,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Myc associated factor X,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc,
http://linkedlifedata.com/resource/pubmed/chemical/TERT protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Telomerase
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
46
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10279-86
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:17705400-Basic-Leucine Zipper Transcription Factors,
pubmed-meshheading:17705400-Circular Dichroism,
pubmed-meshheading:17705400-Cross-Linking Reagents,
pubmed-meshheading:17705400-DNA,
pubmed-meshheading:17705400-Dimerization,
pubmed-meshheading:17705400-E-Box Elements,
pubmed-meshheading:17705400-Electrophoretic Mobility Shift Assay,
pubmed-meshheading:17705400-Humans,
pubmed-meshheading:17705400-Microscopy, Atomic Force,
pubmed-meshheading:17705400-Nucleic Acid Conformation,
pubmed-meshheading:17705400-Promoter Regions, Genetic,
pubmed-meshheading:17705400-Protein Binding,
pubmed-meshheading:17705400-Protein Structure, Quaternary,
pubmed-meshheading:17705400-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:17705400-Telomerase
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pubmed:year |
2007
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pubmed:articleTitle |
Direct visualization of the binding of c-Myc/Max heterodimeric b-HLH-LZ to E-box sequences on the hTERT promoter.
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pubmed:affiliation |
Département de pharmacologie, Faculté de médecine et des sciences de la santé, Université de Sherbrooke, Sherbrooke, QC, Canada J1H 5N4.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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