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Article

Analysis of primary structural determinants that distinguish the centromere-specific function of histone variant Cse4p from histone H3.

Molecular and cellular biology - 1 Sept 1999

Keith K C, Baker R E, Chen Y, Harris K, Stoler S, Fitzgerald-Hayes M

Abstract excerpt

Cse4p is a variant of histone H3 that has an essential role in chromosome segregation and centromere chromatin structure in budding yeast. Cse4p has a unique 135-amino-acid N terminus and a C-terminal histone-fold domain that is more than 60% identical to histone H3 and the mammalian centromere protein CENP-A. Cse4p and CENP-A have biochemical properties similar to H3 and probably replace H3 in...

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Identifiers

PMID: 10454560
DOI: 10.1128/MCB.19.9.6130
PMCID: PMC84538

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Analysis of primary structural determinants that distinguish the centromere-specific function of histone variant Cse4p from histone H3.PMID 10454560Read ↗

The N terminus of the centromere H3-like protein Cse4p performs an essential function distinct from that of the histone fold domain.Semantic proximity Read ↗

The histone fold domain of Cse4 is sufficient for CEN targeting and propagation of active centromeres in budding yeast.Semantic proximity Read ↗

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