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Histone-histone interactions and centromere function
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DOI：10.1128/MCB.20.15.5700-5711.2000.png)
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摘要
En 中文
Cse4p is a structural component of the core centromere of Saccharomyces cerevisiae and is a member of the conserved CENP-A family of specialized histone H3 variants. The histone H4 allele hhf1-20 confers defects in core centromere chromatin structure and mitotic chromosome transmission. We have proposed that Cse4p and histone H4 interact through their respective histone fold domains to assemble a nucleosome-like structure at centromeric DNA. To test this model, we targeted random mutations to the Cse4p histone fold domain and isolated three temperature-sensitive cse4 alleles in an unbiased genetic screen. Two of the cse4 alleles contain mutations at the Cse4p-H4 interface. One of these requires two widely separated mutations demonstrating long-range cooperative interactions in the structure. The third cse4 allele is mutated at its helix 2-helix 3 interface, a region required for homotypic H3 fold dimerization, Overexpression of wild-type Cse4p and histone H4 confer reciprocal allele-specific suppression of cse4 and hhf1 mutations, providing strong evidence for Cse4p-H4 protein interaction. Overexpression of histone H3 is dosage lethal in cse4 mutants, suggesting that histone H3 competes with Cse4p for histone H4 binding. However, the relative resistance of the Cse4p-H4 pathway to H3 interference argues that centromere chromatin assembly must be highly regulated.
Keyword:
SACCHAROMYCES-CEREVISIAE KINETOCHORE
MITOTIC CHROMOSOME TRANSMISSION
CELL-CYCLE PROGRESSION
BUDDING YEAST
CENP-A
CHROMATIN STRUCTURE
NUCLEOSOMAL DNA
CROSS-LINKING
IN-VIVO
PROTEIN
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期刊
IF:
2.7
论文数:
1.3W
被引数:
3.8W
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