NF-Y is a trimeric CCAAT-binding factor with histone fold subunits (NF-YB/NF-YC) and bipartite activation domains located on NF-YA and NF-YC, We reconstituted the NF-Y activation potential in vivo with GAL4 DBD fusions, In the GAL4-YA configuration, activation requires co-expression of the three subunits; with GAL4-YB and GAL4-YC, transfections of the histone fold partners are sufficient, provided that the Q-rich domain of NF-YC is present, Combinations of mutants indicate that the Q-rich domains of NF-YA and NF-YC are redundant in the trimeric complex, Glutamines 101 and 102 of NF-YA are required for activity, We assayed NF-Y on different promoter targets, containing single or multiple GAL4 sites: whereas on a single site NF-Y is nearly as powerful as VP16, on multiple sites neither synergistic nor additive effects are observed, NF-Y activates TATA and Inr core elements and the overall potency is in the same range as other Q-rich and Pro-rich activation domains. These results represent the first in vivo evidence of subunit interactions studies and further support the hypothesis that NF-Y is a general promoter organizer rather than a brute activator.

Dissection of the NF-Y transcriptional activation potential / DI SILVIO, Alberto; Imbriano, Carol; Mantovani, Roberto. - In: NUCLEIC ACIDS RESEARCH. - ISSN 0305-1048. - STAMPA. - 27 (13)(1999), pp. 2578-2584. [10.1093/nar/27.13.2578]

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