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http://purl.uniprot.org/citations/15598823http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15598823http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15598823http://www.w3.org/2000/01/rdf-schema#comment"Chromatin is regulated at many different levels, from higher-order packing to individual nucleosome placement. Recent studies have shown that individual histone modifications, and combinations thereof, play a key role in modulating chromatin structure and gene activity. Reported here is an analysis of Arabidopsis histone H3 modifications by nanoflow-HPLC coupled to electrospray ionization on a hybrid linear ion trap-Fourier transform mass spectrometer (LTQ/FTMS). We find that the sites of acetylation and methylation, in general, correlate well with other plants and animals. Two well-studied modifications, dimethylation of Lys-9 (correlated with silencing) and acetylation of Lys-14 (correlated with active chromatin) while abundant by themselves were rarely found on the same histone H3 tail. In contrast, dimethylation at Lys-27 and monomethylation at Lys-36 were commonly found together. Interestingly, acetylation at Lys-9 was found only in a low percentage of histones while acetylation of Lys-14 was very abundant. The two histone H3 variants, H3.1 and H3.2, also differ in the abundance of silencing and activating marks confirming other studies showing that the replication-independent histone H3 is enriched in active chromatin."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkh992"xsd:string
http://purl.uniprot.org/citations/15598823http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkh992"xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Johnson L."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Johnson L."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Hunt D.F."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Hunt D.F."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Shabanowitz J."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Shabanowitz J."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Garcia B.A."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Garcia B.A."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Jacobsen S.E."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Jacobsen S.E."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Mollah S."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Mollah S."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Muratore T.L."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/author"Muratore T.L."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/pages"6511-6518"xsd:string
http://purl.uniprot.org/citations/15598823http://purl.uniprot.org/core/pages"6511-6518"xsd:string