| First Author | Bolognese F | Year | 2000 |
| Journal | Nucleic Acids Res | Volume | 28 |
| Issue | 19 | Pages | 3830-8 |
| PubMed ID | 11000277 | Mgi Jnum | J:65020 |
| Mgi Id | MGI:1891584 | Doi | 10.1093/nar/28.19.3830 |
| Citation | Bolognese F, et al. (2000) Cloning and characterization of the histone-fold proteins YBL1 and YCL1. Nucleic Acids Res 28(19):3830-8 |
| abstractText | 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. |
