Nucleic Acids Research, 2000, Vol. 28, No. 19 3830-3838
© 2000 Oxford University Press
Cloning and characterization of the histone-fold proteins YBL1 and YCL1
Dipartimento di Genetica e Biologia dei Microrganismi, Università di Milano, Via Celoria 26, 20133 Milano, Italy and 1Dipartimento di Biologia Animale, Università di Modena e Reggio, Via Campi 213, 41100 Modena, Italy
Histones are among the most conserved proteins in evolution, sharing a histone fold motif. A number of additional histonic proteins exist and are involved in the process of transcriptional regulation. We describe here the identification, cloning and characterization of two small members of the H2A–H2B sub-family (YBL1 and YCL1) related to the NF-YB and NF-YC subunits of the CCAAT-binding activator NF-Y and to the TATA-binding protein (TBP) binding repressor NC2. Unlike the latters, YBL1 and YCL1 have no intrinsic CCAAT or TATA-binding capacity. In nucleosome reconstitution assays, they can form complexes with histones in solution and on DNA and they are part of relatively large complexes, as determined by glycerol gradient experiments. Our data support the idea that YBL1 and YCL1 are divergent with respect to NF-YB and NF-YC for specific functions, but have coevolved the capacity to interact with nucleosomal structures.
* To whom correspondence should be addressed. Tel: +39 (0)59 2055542; Fax: +39 (0)59 2055548; Email: mantor@mail.unimo.it The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
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