4AWL

The NF-Y transcription factor is structurally and functionally a sequence specific histone

Summary for 4AWL

• Entry DOI: 10.2210/pdb4awl/pdb
• Related: 1N1J
• Descriptor: NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT ALPHA, NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT BETA, NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT GAMMA, ... (6 entities in total)
• Functional Keywords: transcription-dna complex, nf-y, dna-binding, transcription/dna
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 5
• Total formula weight: 46645.28

Authors

Nardini, M.,Gnesutta, N.,Donati, G.,Gatta, R.,Forni, C.,Fossati, A.,Vonrhein, C.,Moras, D.,Romier, C.,Mantovani, R.,Bolognesi, M. (deposition date: 2012-06-04, release date: 2013-01-30, Last modification date: 2023-12-20)

Primary citation

Nardini, M.,Gnesutta, N.,Donati, G.,Gatta, R.,Forni, C.,Fossati, A.,Vonrhein, C.,Moras, D.,Romier, C.,Bolognesi, M.,Mantovani, R.
Sequence-Specific Transcription Factor NF-Y Displays Histone-Like DNA Binding and H2B-Like Ubiquitination.
Cell(Cambridge,Mass.), 152:132-, 2013

PubMed 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.

PubMed: 23332751
DOI: 10.1016/J.CELL.2012.11.047

Experimental method

X-RAY DIFFRACTION (3.08 Å)