NF-Y transcription factor comprises three subunits; NF-YA, NF-YB, and NF-YC. NF-YB and NF-YC dimerize through their histone fold domain (HFD), which can bind DNA in a non-sequence-specific fashion while serving as a scaffold for NF-YA trimerization. Upon trimerization, NF-YA specifically recognizes the CCAAT box sequence on promoters and enhancers. In plants, each NF-Y subunit is encoded by several genes giving rise to hundreds of potential heterotrimeric combinations. In addition, plant NF-YBs and NF-YCs interact with other protein partners to recognize a plethora of genomic motifs, as the CCT protein family that binds CORE sites. The NF-Y subunit organization and its DNA-binding properties, together with the NF-Y HFD capacity to adapt different protein modules, represent plant-specific features that play a key role in development, growth and reproduction. Despite their relevance, these features are still poorly understood at the molecular level. Here, we present the structures of Arabidopsis and rice NF-YB/NF-YC dimers, and of an Arabidopsis NF-Y trimer in complex with the FT CCAAT box, together with biochemical data on NF-Y mutants. The dimeric structures identify the key residues for NF-Y HFD stabilization. The NF-Y/DNA structure and the mutation experiments shed light on HFD trimerization interface properties and the NF-YA sequence appetite for the bases flanking the CCAAT motif. These data explain the logic of plant NF-Y gene expansion: the trimerization adaptability and the flexible DNA-binding rules serve the scopes of accommodating the large number of NF-YAs, CCTs and possibly other NF-Y HFD binding partners and a diverse audience of genomic motifs.

Structural determinants for NF-Y subunit organization and NF-Y/DNA association in plants / A. Chaves-Sanjuan, N. Gnesutta, A. Gobbini, D. Martignago, A. Bernardini, F. Fornara, R. Mantovani, M. Nardini. - In: PLANT JOURNAL. - ISSN 0960-7412. - 105:1(2021 Jan), pp. 49-61. [10.1111/tpj.15038]

Structural determinants for NF-Y subunit organization and NF-Y/DNA association in plants

A. Chaves-Sanjuan
Primo
;
N. Gnesutta
Secondo
;
D. Martignago;A. Bernardini;F. Fornara;R. Mantovani
Penultimo
;
M. Nardini
Ultimo
2021-01

Abstract

NF-Y transcription factor comprises three subunits; NF-YA, NF-YB, and NF-YC. NF-YB and NF-YC dimerize through their histone fold domain (HFD), which can bind DNA in a non-sequence-specific fashion while serving as a scaffold for NF-YA trimerization. Upon trimerization, NF-YA specifically recognizes the CCAAT box sequence on promoters and enhancers. In plants, each NF-Y subunit is encoded by several genes giving rise to hundreds of potential heterotrimeric combinations. In addition, plant NF-YBs and NF-YCs interact with other protein partners to recognize a plethora of genomic motifs, as the CCT protein family that binds CORE sites. The NF-Y subunit organization and its DNA-binding properties, together with the NF-Y HFD capacity to adapt different protein modules, represent plant-specific features that play a key role in development, growth and reproduction. Despite their relevance, these features are still poorly understood at the molecular level. Here, we present the structures of Arabidopsis and rice NF-YB/NF-YC dimers, and of an Arabidopsis NF-Y trimer in complex with the FT CCAAT box, together with biochemical data on NF-Y mutants. The dimeric structures identify the key residues for NF-Y HFD stabilization. The NF-Y/DNA structure and the mutation experiments shed light on HFD trimerization interface properties and the NF-YA sequence appetite for the bases flanking the CCAAT motif. These data explain the logic of plant NF-Y gene expansion: the trimerization adaptability and the flexible DNA-binding rules serve the scopes of accommodating the large number of NF-YAs, CCTs and possibly other NF-Y HFD binding partners and a diverse audience of genomic motifs.
Arabidopsis thaliana; Oryza sativa; CCAAT box; CCT; CONSTANS; Ghd8; NF-Y; Transcription factor; flowering; histone fold
Settore BIO/10 - Biochimica
Settore BIO/18 - Genetica
Settore BIO/04 - Fisiologia Vegetale
CONSTANS companions: imparting sequence-specificity to histone-like proteins in plants
nov-2020
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/793667
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