Abstract
Centromeres are the differentiated chromosomal domains that specify the mitotic behavior of chromosomes. To examine the molecular basis for the specification of centromeric chromatin, we have cloned a human cDNA that encodes the 17-kD histone-like centromere antigen, CENP-A. Two domains are evident in the 140 aa CENP-A polypeptide: a unique NH2-terminal domain and a 93-amino acid COOH-terminal domain that shares 62% identity with nucleosomal core protein, histone H3. An epitope tagged derivative of CENP-A was faithfully targeted to centromeres when expressed in a variety of animal cells and this targeting activity was shown to reside in the histone-like COOH-terminal domain of CENP-A. These data clearly indicate that the assembly of centromeres is driven, at least in part, by the incorporation of a novel core histone into centromeric chromatin.
Dates
Type | When |
---|---|
Created | 21 years, 3 months ago (May 14, 2004, 8:22 p.m.) |
Deposited | 2 years, 1 month ago (July 22, 2023, 1:41 a.m.) |
Indexed | 2 weeks, 6 days ago (Aug. 6, 2025, 8:11 a.m.) |
Issued | 30 years, 9 months ago (Nov. 1, 1994) |
Published | 30 years, 9 months ago (Nov. 1, 1994) |
Published Online | 30 years, 9 months ago (Nov. 1, 1994) |
Published Print | 30 years, 9 months ago (Nov. 1, 1994) |
@article{Sullivan_1994, title={Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere.}, volume={127}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.127.3.581}, DOI={10.1083/jcb.127.3.581}, number={3}, journal={The Journal of cell biology}, publisher={Rockefeller University Press}, author={Sullivan, K F and Hechenberger, M and Masri, K}, year={1994}, month=nov, pages={581–592} }