<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ragunathan, Kaushik</style></author><author><style face="normal" font="default" size="100%">Jih, Gloria</style></author><author><style face="normal" font="default" size="100%">Moazed, Danesh</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Epigenetics. Epigenetic inheritance uncoupled from sequence-specific recruitment.</style></title><secondary-title><style face="normal" font="default" size="100%">Science</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Science</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adenine</style></keyword><keyword><style  face="normal" font="default" size="100%">Catalytic Domain</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Cycle Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Epigenesis, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Fungal</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, Reporter</style></keyword><keyword><style  face="normal" font="default" size="100%">Heterochromatin</style></keyword><keyword><style  face="normal" font="default" size="100%">Histones</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Lysine</style></keyword><keyword><style  face="normal" font="default" size="100%">Methyltransferases</style></keyword><keyword><style  face="normal" font="default" size="100%">Nuclear Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Operator Regions, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Processing, Post-Translational</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombinant Fusion Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Repressor Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Schizosaccharomyces</style></keyword><keyword><style  face="normal" font="default" size="100%">Schizosaccharomyces pombe Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Tetracycline</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2015 Apr 3</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/25831549</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">348</style></volume><pages><style face="normal" font="default" size="100%">1258699</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Changes in histone posttranslational modifications are associated with epigenetic states that define distinct patterns of gene expression. It remains unclear whether epigenetic information can be transmitted through histone modifications independently of specific DNA sequence, DNA methylation, or RNA interference. Here we show that, in the fission yeast Schizosaccharomyces pombe, ectopically induced domains of histone H3 lysine 9 methylation (H3K9me), a conserved marker of heterochromatin, are inherited through several mitotic and meiotic cell divisions after removal of the sequence-specific initiator. The putative JmjC domain H3K9 demethylase, Epe1, and the chromodomain of the H3K9 methyltransferase, Clr4/Suv39h, play opposing roles in maintaining silent H3K9me domains. These results demonstrate how a direct &quot;read-write&quot; mechanism involving Clr4 propagates histone modifications and allows histones to act as carriers of epigenetic information.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">6230</style></issue><notes><style face="normal" font="default" size="100%">http://www.sciencemag.org/content/early/2014/11/19/science.1258699</style></notes><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/25831549?dopt=Abstract</style></custom1></record></records></xml>