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Molecular and Cellular Biology, December 1999, p. 8591-8603, Vol. 19, No. 12
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

NF-Y Associates with H3-H4 Tetramers and Octamers by Multiple Mechanisms

Giuseppina Caretti,1 Maria Carla Motta,1,dagger and Roberto Mantovani1,2,*

Dipartimento di Genetica e Biologia dei Microrganismi, Università di Milano, 20133 Milan,1 and Dipartimento di Biologia Animale, Università di Modena e Reggio, 41100 Modena,2 Italy

Received 12 May 1999/Returned for modification 23 June 1999/Accepted 16 August 1999

NF-Y is a CCAAT-binding trimer with two histonic subunits, NF-YB and NF-YC, resembling H2A-H2B. We previously showed that the short conserved domains of NF-Y efficiently bind to the major histocompatibility complex class II Ea Y box in DNA nucleosomized with purified chicken histones. Using wild-type NF-Y and recombinant histones, we find that NF-Y associates with H3-H4 early during nucleosome assembly, under conditions in which binding to naked DNA is not observed. In such assays, the NF-YB-NF-YC dimer forms complexes with H3-H4, for whose formation the CCAAT box is not required. We investigated whether they represent octamer-like structures, using DNase I, micrococcal nuclease, and exonuclease III, and found a highly positioned nucleosome on Ea, whose boundaries were mapped; addition of NF-YB-NF-YC does not lead to the formation of octameric structures, but changes in the digestion patterns are observed. NF-YA can bind to such preformed DNA complexes in a CCAAT-dependent way. In the absence of DNA, NF-YB-NF-YC subunits bind to H3-H4, but not to H2A-H2B, through the NF-YB histone fold. These results indicate that (i) the NF-Y histone fold dimer can efficiently associate DNA during nucleosome formation; (ii) it has an intrinsic affinity for H3-H4 but does not form octamers; and (iii) the interactions between NF-YA, NF-YB-NF-YC, and H3-H4 or nucleosomes are not mutually exclusive. Thus, NF-Y can intervene at different steps during nucleosome formation, and this scenario might be paradigmatic for other histone fold proteins involved in gene regulation.

* Corresponding author. Mailing address: Dipartimento di Genetica e Biologia dei Microrganismi, Università di Milano, Via Celoria 26, 20133 Milan, Italy. Phone: 39-2-26605239. Fax: 39-2-2664551. E-mail: mantor{at}imiucca.csi.unimi.it.

dagger Present address: Nederlands Kanker Institut, 1066 CX Amsterdam, The Netherlands.

Molecular and Cellular Biology, December 1999, p. 8591-8603, Vol. 19, No. 12
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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