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 α 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.

Sequence-specific transcription factor NF-Y displays histone-like DNA binding and H2B-like ubiquitination / M. Nardini, N. Gnesutta, G. Donati, R. Gatta, C. Forni, A. Fossati, C. Vonrhein, D. Moras, C. Romier, M. Bolognesi, R. Mantovani. - In: CELL. - ISSN 0092-8674. - 152:1/2(2013), pp. 132-143. [10.1016/j.cell.2012.11.047]

Sequence-specific transcription factor NF-Y displays histone-like DNA binding and H2B-like ubiquitination

M. Nardini
Primo
;
N. Gnesutta;G. Donati;R. Gatta;C. Forni;A. Fossati;M. Bolognesi
;
R. Mantovani
2013

Abstract

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 α 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.
Settore BIO/10 - Biochimica
Settore BIO/18 - Genetica
2013
http://hdl.handle.net/2434/506216
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/221889
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