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Originally published In Press as doi:10.1074/jbc.M304606200 on May 27, 2003
J. Biol. Chem., Vol. 278, Issue 33, 30435-30440, August 15, 2003
Dynamic Recruitment of NF-Y and Histone Acetyltransferases on Cell-cycle Promoters*
Giuseppina Caretti ¶,
Valentina Salsi ,
Chiara Vecchi ,
Carol Imbriano and
Roberto Mantovani ** 
From the
Dipartimento di Biologia Animale,
Università di Modena e Reggio, Via Campi 213/d, 41100 Modena, Italy and
the **Dipartimento di Scienze Biomolecolari e
Biotechnologiche, Università di Milano, Via Celoria 26, 20133 Milano,
Italy
Regulation of transcription during the cell-cycle is under the control of
E2 factors (E2Fs), often in cooperation with nuclear factor Y (NF-Y), a
histone-like CCAAT-binding trimer. NF-Y is paradigmatic of a constitutive,
ubiquitous factor that pre-sets the promoter architecture for other regulatory
proteins to access it. We analyzed the recruitment of NF-Y, E2F1/4/6, histone
acetyltransferases, and histone deacetylase (HDAC) 1/3/4 to several cell-cycle
promoters by chromatin immunoprecipitation assays in serum-starved and
restimulated NIH3T3 cells. NF-Y binding is not constitutive but timely
regulated in all promoters tested, being displaced when promoters are
repressed. p300 association correlates with activation, and it is never found
in the absence of NF-Y, whereas PCAF/hGCN5 is often found before NF-Y
association. E2F4 and E2F6, together with HDACs, are bound to repressed
promoters, including the G2/M Cyclin B2. As expected, an inverse
relationship between HDACs association and histones H3/H4 acetylation is
observed. Blocking cells in G1 with the cyclin-dependent kinase 2
inhibitor R-roscovitine confirms that NF-Y is bound to G1/S but not
to G2/M promoters in G1. These data indicate that
following the release of E2Fs/HDACs, a hierarchy of PCAF-NF-Y-p300
interactions and H3-H4 acetylations are required for activation of cell-cycle
promoters.
Received for publication, May 2, 2003
* This work was supported by grants from Associazione Italiana Ricerca sul
Cancro and Progetto di Rilevante Interesse Nazionale-Ministero
Università e Ricerca Scientifica (to R. M.). The costs of publication
of this article were defrayed in part by the payment of page charges. This
article must therefore be hereby marked "advertisement"
in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Recipients of Fondazione Italiana Ricerca sul Cancro fellowships.
¶ Present address: National Institutes of Health, Bethesda, MD.

To whom correspondence should be addressed: Dipartimento di Scienze
Biomolecolari e Biotechnologiche, Via Celoria 26, 20133 Milano, Italy. Tel.:
39-02-50315005; Fax: 39-02-50315044; E-mail:
mantor{at}unimi.it.

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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
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