Abstract
CENP-A, the centromere-specific histone H3 variant, plays a crucial role in organizing kinetochore chromatin for precise chromosome segregation. We have isolated Ams2, a Daxx-like motif-containing GATA factor, and histone H4, as multicopy suppressors of cnp1-1, an S. pombe CENP-A mutant. While depletion of Ams2 results in the reduction of CENP-A binding to the centromere and chromosome missegregation, increasing its dosage restores association of a CENP-A mutant protein with centromeres. Conversely, overexpression of CENP-A or histone H4 suppresses an ams2 disruptant. The intracellular amount of Ams2 thus affects centromeric nucleosomal constituents. Ams2 is abundant in S phase and associates with chromatin, including the central centromeres through binding to GATA-core sequences. Ams2 is thus a cell cycle-regulated GATA factor that is required for centromere function.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Cell Cycle / physiology*
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Centromere / metabolism*
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Chromosomal Proteins, Non-Histone / metabolism*
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Chromosomes / genetics
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Chromosomes / metabolism
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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GATA Transcription Factors
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Histones / metabolism
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Humans
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In Situ Hybridization, Fluorescence
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Molecular Sequence Data
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Phenotype
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Protein Binding
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Schizosaccharomyces / cytology
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Schizosaccharomyces / physiology*
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Schizosaccharomyces pombe Proteins / chemistry
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Schizosaccharomyces pombe Proteins / genetics
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Schizosaccharomyces pombe Proteins / metabolism*
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Sequence Alignment
Substances
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Ams2 protein, S pombe
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Chromosomal Proteins, Non-Histone
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Cnp1 protein, S pombe
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DNA-Binding Proteins
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GATA Transcription Factors
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Histones
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Schizosaccharomyces pombe Proteins