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Distinct protein interaction domains and protein spreading in a complex centromere

Open access
Partridge, Janet F., Borgstrøm, Britta, Allshire, Robin C.·2000·Genes & Development

Abstract

Fission yeast (Schizosaccharomyces pombe) centromeres are composed of large (40–100 kb) inverted repeats that display heterochromatic features, thus providing a good model for higher eukaryotic centromeres. The association of three proteins that mediate region-specific silencing across centromere 1 has been mapped by quantitative chromatin immunoprecipitation. Swi6 and Chp1 are confined to the flanking outer repeats and Swi6 can spread across at least 3 kb of extraneous chromatin in cen1. In contrast, Mis6 coats the inner repeats and central core. tRNA genes demarcate this transition zone. These analyses clearly define two distinct domains within this complex centromere which interact with different proteins.

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Metadata

Authors
Partridge, J. F., Borgstrøm, B., & Allshire, R. C.
Venue
Genes & Development
Published
2000-04-01
Volume
14
Issue
7
Pages
783-791
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
OpenAlex
W2141764062
Cited by
242
References
0
Type
posted content
Language
en
Open access
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CoChat. (2026). Citation check: Distinct protein interaction domains and protein spreading in a complex centromere. https://app.cochat.ai/papers/10.1101/gad.14.7.783
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Partridge, J. F., Borgstrøm, B., & Allshire, R. C. (2000). Distinct protein interaction domains and protein spreading in a complex centromere. Genes & Development. https://doi.org/10.1101/gad.14.7.783

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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