ArticleMolecular and cellular biology2000
The N terminus of the centromere H3-like protein Cse4p performs an essential function distinct from that of the histone fold domain.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed, 149 citations in OpenAlex.
- Keeping it centered: decoding the activities that regulate yeast histone H3 variant Cse4 and confine it to centromeres.Frontiers in cell and developmental biology · 2026Review
- Evidence of centromeric histone 3 chaperone involved in DNA damage repair pathway in budding yeast.eLife · 2025Article
- Dynamic sperm proteome remodeling during epididymal maturation in a marsupial, Macropus giganteus†.Biology of reproduction · 2025Article
- Modeling the START transition in the budding yeast cell cycle.PLoS computational biology · 2024Article
- Recognition of centromere-specific histone Cse4 by the inner kinetochore Okp1-Ame1 complex.EMBO reports · 2023Article
- Misregulation of cell cycle-dependent methylation of budding yeast CENP-A contributes to chromosomal instability.Molecular biology of the cell · 2023Article
- Cryo-EM structure of the complete inner kinetochore of the budding yeast point centromere.Science advances · 2023Article
- Cdc7-mediated phosphorylation of Cse4 regulates high-fidelity chromosome segregation in budding yeast.Molecular biology of the cell · 2021Article
- The N-terminal tail ofMolecular biology of the cell · 2021Article
- Centromere Engineering as an Emerging Tool for Haploid Plant Production: Advances and Challenges.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Conservation of centromeric histone 3 interaction partners in plants.Journal of experimental botany · 2020Article
- Skp, Cullin, F-box (SCF)-Met30 and SCF-Cdc4-Mediated Proteolysis of CENP-A Prevents Mislocalization of CENP-A for Chromosomal Stability in Budding Yeast.PLoS genetics · 2020Article
- Article
- Localization of Drosophila CENP-A to non-centromeric sites depends on the NuRD complex.Nucleic acids research · 2019Article
- The COMA complex interacts with Cse4 and positions Sli15/Ipl1 at the budding yeast inner kinetochore.eLife · 2019Article
- Novel genetic tools for probing individual H3 molecules in each nucleosome.Current genetics · 2019Review
- Cell cycle-dependent association of polo kinase Cdc5 with CENP-A contributes to faithful chromosome segregation in budding yeast.Molecular biology of the cell · 2019Article
- Conformational flexibility of histone variant CENP-AThe Journal of biological chemistry · 2018Article
- A Genome-Wide Screen Reveals a Role for the HIR Histone Chaperone Complex in Preventing Mislocalization of Budding Yeast CENP-A.Genetics · 2018Article
- An asymmetric centromeric nucleosome.eLife · 2018Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Cse4p is an evolutionarily conserved histone H3-like protein that is thought to replace H3 in a specialized nucleosome at the yeast (Saccharomyces cerevisiae) centromere. All known yeast, worm, fly, and human centromere H3-like proteins have highly conserved C-terminal histone fold domains (HFD) but very different N termini. We have carried out a comprehensive and systematic mutagenesis of the Cse4p N terminus to analyze its function. Surprisingly, only a 33-amino-acid domain within the 130-amino-acid-long N terminus is required for Cse4p N-terminal function. The spacing of the essential N-terminal domain (END) relative to the HFD can be changed significantly without an apparent effect on Cse4p function. The END appears to be important for interactions between Cse4p and known kinetochore components, including the Ctf19p/Mcm21p/Okp1p complex. Genetic and biochemical evidence shows that Cse4p proteins interact with each other in vivo and that nonfunctional cse4 END and HFD mutant proteins can form functional mixed complexes. These results support different roles for the Cse4p N terminus and the HFD in centromere function and are consistent with the proposed Cse4p nucleosome model. The structure-function characteristics of the Cse4p N terminus are relevant to understanding how other H3-like proteins, such as the human homolog CENP-A, function in kinetochore assembly and chromosome segregation.
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