ArticleMolecular and cellular biology1999
Analysis of primary structural determinants that distinguish the centromere-specific function of histone variant Cse4p from histone H3.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
50 citing papers in PubMed, 82 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
- Humanization reveals pervasive incompatibility of yeast and human kinetochore components.G3 (Bethesda, Md.) · 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
- Methylation of CENP-A/Cse4 on arginine 143 and lysine 131 regulates kinetochore stability in yeast.Genetics · 2023Article
- Cdc7-mediated phosphorylation of Cse4 regulates high-fidelity chromosome segregation in budding yeast.Molecular biology of the cell · 2021Article
- Functional and Comparative Analysis of Centromeres Reveals Clade-Specific Genome Rearrangements inmBio · 2021Article
- Biochemical evidence for diverse strategies in the inner kinetochore.Open biology · 2020Review
- Epigenetic regulation of centromere function.Cellular and molecular life sciences : CMLS · 2020Review
- Seeing is believing: our evolving view of kinetochore structure, composition, and assembly.Current opinion in cell biology · 2019Review
- The COMA complex interacts with Cse4 and positions Sli15/Ipl1 at the budding yeast inner kinetochore.eLife · 2019Article
- 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
- The kinetochore module Okp1The EMBO journal · 2019Article
- Conformational flexibility of histone variant CENP-AThe Journal of biological chemistry · 2018Article
- An asymmetric centromeric nucleosome.eLife · 2018Article
- Degradation of centromeric histone H3 variant Cse4 requires the Fpr3 peptidyl-prolyl Cis-Trans isomerase.Genetics · 2014Article
- Centromere-like regions in the budding yeast genome.PLoS genetics · 2013Article
- SWI/SNF-like chromatin remodeling factor Fun30 supports point centromere function in S. cerevisiae.PLoS genetics · 2012Article
- Methylation of CenH3 arginine 37 regulates kinetochore integrity and chromosome segregation.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Molecular underpinnings of centromere identity and maintenance.Trends in biochemical sciences · 2012Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
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 centromere-specific nucleosomes in yeasts and mammals, respectively. In order to identify regions of Cse4p that distinguish it from H3 and confer centromere function, a systematic site-directed mutational analysis was performed. Nested deletions of the Cse4p N terminus showed that this region of the protein contains at least one essential domain. The C-terminal histone-fold domain of Cse4p was analyzed by changing Cse4p amino acids that differ between Cse4p and H3 to the analogous H3 residues. Extensive substitution of contiguous Cse4p residues with H3 counterparts resulted in cell lethality. However, all large lethal substitution alleles could be subdivided into smaller viable alleles, many of which caused elevated rates of mitotic chromosome loss. The results indicate that residues critical for wild-type Cse4p function and high-fidelity chromosome transmission are distributed across the entire histone-fold domain. Our findings are discussed in the context of the known structure of H3 within the nucleosome and compared with previous results reported for CENP-A.
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