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Publication : Heterochromatic deposition of centromeric histone H3-like proteins.

First Author  Henikoff S Year  2000
Journal  Proc Natl Acad Sci U S A Volume  97
Issue  2 Pages  716-21
PubMed ID  10639145 Mgi Jnum  J:59895
Mgi Id  MGI:1352277 Doi  10.1073/pnas.97.2.716
Citation  Henikoff S, et al. (2000) Heterochromatic deposition of centromeric histone H3-like proteins. Proc Natl Acad Sci U S A 97(2):716-21
abstractText  Centromeres of most organisms are embedded within constitutive heterochromatin, the condensed regions of chromosomes that account for a large fraction of complex genomes. The functional significance of this centromere-heterochromatin relationship, if any, is unknown. One possibility is that heterochromatin provides a suitable environment for assembly of centromere components, such as special centromeric nucleosomes that contain distinctive histone H3-like proteins. We describe a Drosophila H3-like protein, Cid (for centromere identifier) that localizes exclusively to fly centromeres. When the cid upstream region drives expression of H3 and H2B histone-green fluorescent protein fusion genes in Drosophila cells, euchromatin-specific deposition results. Remarkably, when the cid upstream region drives expression of yeast, worm, and human centromeric histone-green fluorescent protein fusion proteins, localization is preferentially within Drosophila pericentric heterochromatin. Heterochromatin-specific localization also was seen for yeast and worm centromeric proteins constitutively expressed in human cells. Preferential localization to heterochromatin in heterologous systems is unexpected if centromere-specific or site-specific factors determine H3-like protein localization to centromeres. Rather, the heterochromatic state itself may help localize centromeric components.
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