Nucleic Acids Research, Vol 27, Issue 13 2578-2584, Copyright © 1999 by Oxford University Press
A de Silvio, C Imbriano and R Mantovani
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.
ARTICLES
Dissection of the NF-Y transcriptional activation potential
Dipartimento di Genetica e Biologia dei Microrganismi, Universita di Milano, Via Celoria 26, 20133 Milano, Italy.
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