دورية أكاديمية
Sequence-specific transcription factor NF-Y displays histone-like DNA binding and H2B-like ubiquitination
| العنوان: | Sequence-specific transcription factor NF-Y displays histone-like DNA binding and H2B-like ubiquitination |
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| المؤلفون: | Nardini, Marco, Gnesutta, Nerina, Gatta, Raffaella, Forni, Claudia, Fossati, Andrea, Vonrhein, Clemens, Moras, Dino, Romier, Christophe, Bolognesi, Martino, Mantovani, Roberto, DONATI, Giacomo |
| المساهمون: | Nardini, Marco, Gnesutta, Nerina, Donati, Giacomo, Gatta, Raffaella, Forni, Claudia, Fossati, Andrea, Vonrhein, Clemen, Moras, Dino, Romier, Christophe, Bolognesi, Martino, Mantovani, Roberto |
| سنة النشر: | 2013 |
| المجموعة: | Università degli studi di Torino: AperTo (Archivio Istituzionale ad Accesso Aperto) |
| مصطلحات موضوعية: | Amino Acid Sequence, Animal, CCAAT-Binding Factor, Crystallography, X-Ray, DNA, HSP72 Heat-Shock Protein, Histone, Human, Molecular Sequence Data, Multiprotein Complexe, Oligonucleotide, Promoter Regions, Genetic, Protein Structure, Tertiary, Sequence Alignment, Ubiquitination, Biochemistry, Genetics and Molecular Biology (all) |
| الوصف: | The sequence-specific transcription factor NF-Y binds the CCAAT box, one of the sequence elements most frequently found in eukaryotic promoters. NF-Y is composed of the NF-YA and NF-YB/NF-YC subunits, the latter two hosting histone-fold domains (HFDs). The crystal structure of NF-Y bound to a 25 bp CCAAT oligonucleotide shows that the HFD dimer binds to the DNA sugar-phosphate backbone, mimicking the nucleosome H2A/H2B-DNA assembly. NF-YA both binds to NF-YB/NF-YC and inserts an a helix deeply into the DNA minor groove, providing sequence-specific contacts to the CCAAT box. Structural considerations and mutational data indicate that NF-YB ubiquitination at Lys138 precedes and is equivalent to H2B Lys120 monoubiquitination, important in transcriptional activation. Thus, NF-Y is a sequence-specific transcription factor with nucleosome-like properties of nonspecific DNA binding and helps establish permissive chromatin modifications at CCAAT promoters. Our findings suggest that other HFD-containing proteins may function in similar ways. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/23332751; info:eu-repo/semantics/altIdentifier/wos/WOS:000313719800012; volume:152; issue:1-2; firstpage:132; lastpage:143; numberofpages:12; journal:CELL; http://hdl.handle.net/2318/1590740Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84872539860 |
| DOI: | 10.1016/j.cell.2012.11.047 |
| الإتاحة: | https://doi.org/10.1016/j.cell.2012.11.047Test http://hdl.handle.net/2318/1590740Test |
| حقوق: | info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.B4585CD1 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1016/j.cell.2012.11.047 |
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