5-Methylcytosine (5mC) and 5-Hydroxymethylcytosine (5hmC) Enhance the DNA Binding of CREB1 to the C/EBP Half-Site Tetranucleotide GCAA.
Identifieur interne : 001421 ( Main/Exploration ); précédent : 001420; suivant : 0014225-Methylcytosine (5mC) and 5-Hydroxymethylcytosine (5hmC) Enhance the DNA Binding of CREB1 to the C/EBP Half-Site Tetranucleotide GCAA.
Auteurs : Khund Sayeed Syed [États-Unis] ; Ximiao He [États-Unis] ; Desiree Tillo [États-Unis] ; Jun Wang [États-Unis] ; Stewart R. Durell [États-Unis] ; Charles Vinson [États-Unis]Source :
- Biochemistry [ 1520-4995 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
- analogues et dérivés : 5-Méthyl-cytosine.
- métabolisme : 5-Méthyl-cytosine, ADN, Protéine de liaison à l'élément de réponse à l'AMP cyclique, Protéines liant les séquences stimulatrices de type CCAAT.
- Animaux, Régions promotrices (génétique), Souris.
English descriptors
- KwdEn :
- MESH :
- chemical , analogs & derivatives : 5-Methylcytosine.
- chemical , metabolism : 5-Methylcytosine, CCAAT-Enhancer-Binding Proteins, Cyclic AMP Response Element-Binding Protein, DNA.
- Animals, Mice, Promoter Regions, Genetic.
Abstract
In human and mouse stem cells and brain, 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC) can occur outside of CG dinucleotides. Using protein binding microarrays (PBMs) containing 60-mer DNA probes, we evaluated the effect of 5mC and 5hmC on one DNA strand on the double-stranded DNA binding of the mouse B-ZIP transcription factors (TFs) CREB1, ATF1, and JUND. 5mC inhibited binding of CREB1 to the canonical CRE half-site |GTCA but enhanced binding to the C/EBP half-site |GCAA. 5hmC inhibited binding of CREB1 to all 8-mers except TGAT|GCAA, where binding is enhanced. We observed similar DNA binding patterns with ATF1, a closely related B-ZIP domain. In contrast, both 5mC and 5hmC inhibited binding of JUND. These results identify new DNA sequences that are well-bound by CREB1 and ATF1 only when they contain 5mC or 5hmC. Analysis of two X-ray structures examines the consequences of 5mC and 5hmC on DNA binding by CREB and FOS|JUN.
DOI: 10.1021/acs.biochem.6b00796
PubMed: 27951657
Affiliations:
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Le document en format XML
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<term>CCAAT-Enhancer-Binding Proteins (metabolism)</term>
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<term>5-Méthyl-cytosine (métabolisme)</term>
<term>ADN (métabolisme)</term>
<term>Animaux</term>
<term>Protéine de liaison à l'élément de réponse à l'AMP cyclique (métabolisme)</term>
<term>Protéines liant les séquences stimulatrices de type CCAAT (métabolisme)</term>
<term>Régions promotrices (génétique)</term>
<term>Souris</term>
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<keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>5-Methylcytosine</term>
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<front><div type="abstract" xml:lang="en">In human and mouse stem cells and brain, 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC) can occur outside of CG dinucleotides. Using protein binding microarrays (PBMs) containing 60-mer DNA probes, we evaluated the effect of 5mC and 5hmC on one DNA strand on the double-stranded DNA binding of the mouse B-ZIP transcription factors (TFs) CREB1, ATF1, and JUND. 5mC inhibited binding of CREB1 to the canonical CRE half-site |GTCA but enhanced binding to the C/EBP half-site |GCAA. 5hmC inhibited binding of CREB1 to all 8-mers except TGAT|GCAA, where binding is enhanced. We observed similar DNA binding patterns with ATF1, a closely related B-ZIP domain. In contrast, both 5mC and 5hmC inhibited binding of JUND. These results identify new DNA sequences that are well-bound by CREB1 and ATF1 only when they contain 5mC or 5hmC. Analysis of two X-ray structures examines the consequences of 5mC and 5hmC on DNA binding by CREB and FOS|JUN.</div>
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