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Title: | Mutation of histone H3 serine 86 disrupts GATA factor Ams2 expression and precise chromosome segregation in fission yeast | Authors: | Lim, K.K Ong, T.Y Tan, Y.R Yang, E.G Ren, B Seah, K.S Yang, Z Tan, T.S Dymock, B.W Chen, E.S |
Keywords: | Ams2 protein, S pombe histone Schizosaccharomyces pombe protein transcription factor GATA amino acid substitution centromere chromosome segregation ectopic expression gene expression regulation genetic transcription genetics metabolism mutation protein synthesis Schizosaccharomyces site directed mutagenesis Amino Acid Substitution Centromere Chromosome Segregation Ectopic Gene Expression GATA Transcription Factors Gene Expression Regulation, Fungal Histones Mutagenesis, Site-Directed Mutation Protein Biosynthesis Schizosaccharomyces Schizosaccharomyces pombe Proteins Transcription, Genetic |
Issue Date: | 2015 | Citation: | Lim, K.K, Ong, T.Y, Tan, Y.R, Yang, E.G, Ren, B, Seah, K.S, Yang, Z, Tan, T.S, Dymock, B.W, Chen, E.S (2015). Mutation of histone H3 serine 86 disrupts GATA factor Ams2 expression and precise chromosome segregation in fission yeast. Scientific reports 5 : 14064. ScholarBank@NUS Repository. https://doi.org/10.1038/srep14064 | Abstract: | Eukaryotic genomes are packed into discrete units, referred to as nucleosomes, by organizing around scaffolding histone proteins. The interplay between these histones and the DNA can dynamically regulate the function of the chromosomal domain. Here, we interrogated the function of a pair of juxtaposing serine residues (S86 and S87) that reside within the histone fold of histone H3. We show that fission yeast cells expressing a mutant histone H3 disrupted at S86 and S87 (hht2-S86AS87A) exhibited unequal chromosome segregation, disrupted transcriptional silencing of centromeric chromatin, and reduced expression of Ams2, a GATA-factor that regulates localization of the centromere-specific histone H3 variant CENP-A. We found that overexpression of ams2(+) could suppress the chromosome missegregation phenotype that arose in the hht2-S86AS87A mutant. We further demonstrate that centromeric localization of SpCENP-A(cnp1-1) was significantly compromised in hht2-S86AS87A, suggesting synergism between histone H3 and the centromere-targeting domain of SpCENP-A. Taken together, our work presents evidence for an uncharacterized serine residue in fission yeast histone H3 that affects centromeric integrity via regulating the expression of the SpCENP-A-localizing Ams2 protein. [173/200 words]. | Source Title: | Scientific reports | URI: | https://scholarbank.nus.edu.sg/handle/10635/175986 | ISSN: | 2045-2322 | DOI: | 10.1038/srep14064 |
Appears in Collections: | Elements Staff Publications |
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