T time for point centromeres

The diverse nature of eukaryotic centromere structure has led to a prevailing view that the kinetochore–chromatin interface is fundamentally different in distinct species. Two studies now challenge this dogma with the identification of budding yeast homologues of the vertebrate centromere DNA-bindin...

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Veröffentlicht in:	Nature cell biology 2012-06, Vol.14 (6), p.559-561
Hauptverfasser:	Gascoigne, Karen E., Cheeseman, Iain M.
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/612/1229 631/80/103/90 631/80/641/1655 Animals Biomedical and Life Sciences Cancer Research Cell Biology Cell cycle Cell Cycle Proteins - metabolism Centromere - metabolism Centromeres Chromosomal Proteins, Non-Histone - metabolism Deoxyribonucleic acid Developmental Biology DNA Genetic aspects Humans Kinetochores - metabolism Life Sciences Microtubule-Associated Proteins - metabolism Microtubules news-and-views Nuclear Proteins - metabolism Physiological aspects Protein-Serine-Threonine Kinases - metabolism Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Stem Cells Vertebrates Yeast Yeast fungi Yeasts
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Beschreibung
Zusammenfassung:	The diverse nature of eukaryotic centromere structure has led to a prevailing view that the kinetochore–chromatin interface is fundamentally different in distinct species. Two studies now challenge this dogma with the identification of budding yeast homologues of the vertebrate centromere DNA-binding proteins CENP-T and CENP-W.
ISSN:	1465-7392 1476-4679
DOI:	10.1038/ncb2509