The MUT9p kinase phosphorylates histone H3 threonine 3 and is necessary for heritable epigenetic silencing in Chlamydomonas
作者： J. A. Casas-Mollano , B.-r. Jeong , J. Xu , H. Moriyama , H. Cerutti
关键词: Biology 、 Histone methylation 、 Histone code 、 Histone methyltransferase 、 Genetics 、 Chromatin remodeling 、 Histone H2A 、 Histone H1 、 Histone phosphorylation 、 Histone H3
摘要: Changes in chromatin organization are emerging as key regulators nearly every aspect of DNA-templated metabolism eukaryotes. Histones undergo many, largely reversible, posttranslational modifications that affect structure. Some modifications, such trimethylation histone H3 on Lys 4 (H3K4me3), correlate with transcriptional activation, whereas others, methylation 27 (H3K27me), associated silent chromatin. Posttranslational may also be involved the inheritance states. Histone phosphorylation has been implicated a variety cellular processes but, because dynamic nature this modification, its potential role long-term gene silencing remained relatively unexplored. We report here Chlamydomonas reinhardtii mutant defective Ser/Thr protein kinase (MUT9p), which phosphorylates histones and H2A, shows deficiencies heritable repression transgenes transposons. Moreover, based immunoprecipitation analyses, phosphorylated H3T3 (H3T3ph) monomethylated H3K4 (H3K4me1) inversely correlated di/trimethylated associate preferentially silenced transcription units. Conversely, loss those marks strains correlates reactivation Our results suggest H3T3ph H3K4me1 function reinforcing epigenetic for euchromatic loci Chlamydomonas.
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