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10.1128/MCB.00112-16 http://scihub22266oqcxt.onion/10.1128/MCB.00112-16 C5086519!5086519 !27550811     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27550811 &cmd=llinks): Failed to open stream: HTTP request failed! 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Combined Action of Histone Reader Modules Regulates NuA4 Local Acetyltransferase Function but Not Its Recruitment on the Genome |pdf=|usr=}}{{27550811 }} gab.com Text Combined Action of Histone Reader Modules Regulates NuA4 Local Acetyltransferase Function but Not Its Recruitment on the Genome JO: Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27550811 #FOAvip Recognition of histone marks by reader modules is thought to be at the heart of epigenetic mechanisms. These protein domains are considered to function by targeting regulators to chromosomal loci carrying specific histone modifications. This is important for proper gene regulation as well as propagation of epigenetic information. The NuA4 acetyltransferase complex contains two of these reader modules, an H3K4me3-specific plant homeodomain (PHD) within the Yng2 subunit and an H3K36me2/3-specific chromodomain in the Eaf3 subunit. While each domain showed a close functional interaction with the respective histone mark that it recognizes, at the biochemical level, genetic level (as assessed with epistatic miniarray profile screens), and phenotypic level, cells with the combined loss of both readers showed greatly enhanced phenotypes. Chromatin immunoprecipitation coupled with next-generation sequencing experiments demonstrated that the Yng2 PHD specifically directs H4 acetylation near the transcription start site of highly expressed genes, while Eaf3 is important downstream on the body of the genes. Strikingly, the recruitment of the NuA4 complex to these loci was not significantly affected. Furthermore, RNA polymerase II occupancy was decreased only under conditions where both PHD and chromodomains were lost, generally in the second half of the gene coding regions. Altogether, these results argue that methylated histone reader modules in NuA4 are not responsible for its recruitment to the promoter or coding regions but, rather, are required to orient its acetyltransferase catalytic site to the methylated histone 3-bearing nucleosomes in the surrounding chromatin, cooperating to allow proper transition from transcription initiation to elongation. Twit Text FOAVip Combined Action of Histone Reader Modules Regulates NuA4 Local Acetyltransferase Function but Not Its Recruitment on the Genome ????Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27550811 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27550811 #FOAvip English Wikipedia <ref>{{Cite pmid|27550811 }}</ref> Combined Action of Histone Reader Modules Regulates NuA4 Local Acetyltransferase Function but Not Its Recruitment on the Genome #MMPMID27550811 Steunou AL ; Cramet M ; Rossetto D ; Aristizabal MJ ; Lacoste N ; Drouin S ; Côté V ; Paquet E ; Utley RT ; Krogan N ; Robert F ; Kobor MS ; Côté J Mol Cell Biol 2016[Nov]; 36 (22 ): 2768-2781 PMID27550811 show ga Recognition of histone marks by reader modules is thought to be at the heart of epigenetic mechanisms. These protein domains are considered to function by targeting regulators to chromosomal loci carrying specific histone modifications. This is important for proper gene regulation as well as propagation of epigenetic information. The NuA4 acetyltransferase complex contains two of these reader modules, an H3K4me3-specific plant homeodomain (PHD) within the Yng2 subunit and an H3K36me2/3-specific chromodomain in the Eaf3 subunit. While each domain showed a close functional interaction with the respective histone mark that it recognizes, at the biochemical level, genetic level (as assessed with epistatic miniarray profile screens), and phenotypic level, cells with the combined loss of both readers showed greatly enhanced phenotypes. Chromatin immunoprecipitation coupled with next-generation sequencing experiments demonstrated that the Yng2 PHD specifically directs H4 acetylation near the transcription start site of highly expressed genes, while Eaf3 is important downstream on the body of the genes. Strikingly, the recruitment of the NuA4 complex to these loci was not significantly affected. Furthermore, RNA polymerase II occupancy was decreased only under conditions where both PHD and chromodomains were lost, generally in the second half of the gene coding regions. Altogether, these results argue that methylated histone reader modules in NuA4 are not responsible for its recruitment to the promoter or coding regions but, rather, are required to orient its acetyltransferase catalytic site to the methylated histone 3-bearing nucleosomes in the surrounding chromatin, cooperating to allow proper transition from transcription initiation to elongation. |*Genome, Fungal [MESH] |Acetylation [MESH] |Acetyltransferases/*chemistry/genetics/metabolism [MESH] |Binding Sites [MESH] |Catalytic Domain [MESH] |Chromatin Immunoprecipitation [MESH] |Epigenesis, Genetic [MESH] |High-Throughput Nucleotide Sequencing [MESH] |Histone Acetyltransferases/chemistry/*metabolism [MESH] |Histone Code [MESH] |Histones/*metabolism [MESH] |Promoter Regions, Genetic [MESH] |RNA Polymerase II/metabolism [MESH] |Saccharomyces cerevisiae Proteins/*chemistry/genetics/*metabolism [MESH] |Saccharomyces cerevisiae/*genetics/metabolism [MESH] |Sequence Analysis, DNA [MESH]Combined Action of Histone Reader Modules Regulates NuA4 Local Acetylt(epmc).pdf DeepDyve Pubget Overpricing