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J. Biol. Chem., Vol. 278, Issue 33, 30435-30440, August 15, 2003

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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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