1: J Biol Chem. 2003 Jan 10;278(2):1336-45. Epub 2002 Oct 24. 

The NF-YB/NF-YC structure gives insight into DNA binding and transcription
regulation by CCAAT factor NF-Y.

Romier C, Cocchiarella F, Mantovani R, Moras D.

Departement de Biologie et Genomique Structurales, Institut de Genetique et de
Biologie Moleculaire et Cellulaire, CNRS/INSERM/Universite Louis Pasteur, 1 Rue
Laurent Fries, B.P. 10142, 67404 Illkirch Cedex, France.

The heterotrimeric transcription factor NF-Y recognizes with high specificity
and affinity the CCAAT regulatory element that is widely represented in
promoters and enhancer regions. The CCAAT box acts in concert with neighboring
elements, and its bending by NF-Y is thought to be a major mechanism required
for transcription activation. We have solved the structure of the NF-YC/NF-YB
subcomplex of NF-Y, which shows that the core domains of both proteins interact
through histone fold motifs. This histone-like pair is closely related to the
H2A/H2B and NC2alpha/NC2beta families, with features that are both common to
this class of proteins and unique to NF-Y. The structure together with the
modeling of the nonspecific interaction of NF-YC/NF-YB with DNA and the full
NF-Y/CCAAT box complex highlight important structural features that account for
different and possibly similar biological functions of the transcriptional
regulators NF-Y and NC2. In particular, it emphasizes the role of the newly
described alphaC helix of NF-YC, which is both important for NF-Y trimerization
and a target for regulatory proteins, such as MYC and p53.

PMID: 12401788 [PubMed - indexed for MEDLINE]


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