Nucleic Acids Research, Vol 25, Issue 11 2174-2181, Copyright © 1997 by Oxford University Press
M Bellorini, DK Lee, JC Dantonel, K Zemzoumi, RG Roeder, L Tora and R Mantovani
Both the TATA and CCAAT boxes are widespread promoter elements and their
binding proteins, TBP and NF-Y, are extremely conserved in evolution. NF-Y
is composed of three subunits, NF-YA, NF-YB and NF-YC, all necessary for
DNA binding. NF-YB and NF-YC contain a putative histone-like motif, a
domain also present in TBP-associated factors (TAFIIs) and in the subunits
of the transcriptional repressor NC2. Immunopurification of holo-TFIID with
anti-TBP and anti-TAFII100 antibodies indicates that a fraction of NF-YB
associates with TFIID in the absence of NF-YA. Sedimentation velocity
centrifugation experiments confirm that two pools of NF-YB, and most likely
NF-YC, exist: one associated with NF-YA and binding to the CCAAT box;
another involved in high molecular weight complexes. We started to dissect
NF-Y-TFIID interactions by showing that: (i) NF-YB and NF-YC interact with
TBP in solution, both separately and once bound to each other; (ii) short
stretches of both NF-YB and NF-YC located within the evolutionary conserved
domains, adjacent to the putative histone fold motifs, are necessary for
TBP binding; (iii) TBP single amino acid mutants in the HS2 helix,
previously shown to be defective in NC2 binding, are also unable to bind
NF-YB and NF-YC.
ARTICLES
CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues
Dipartimento di Genetica e Biologia dei Microrganismi, Universita di Milano, Via Celoria 26, 20133 Milano, Italy.
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