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      HistoneDB 2.0: a histone database with variants—an integrated resource to explore histones and their variants

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          Abstract

          Compaction of DNA into chromatin is a characteristic feature of eukaryotic organisms. The core (H2A, H2B, H3, H4) and linker (H1) histone proteins are responsible for this compaction through the formation of nucleosomes and higher order chromatin aggregates. Moreover, histones are intricately involved in chromatin functioning and provide a means for genome dynamic regulation through specific histone variants and histone post-translational modifications. ‘HistoneDB 2.0 – with variants’ is a comprehensive database of histone protein sequences, classified by histone types and variants. All entries in the database are supplemented by rich sequence and structural annotations with many interactive tools to explore and compare sequences of different variants from various organisms. The core of the database is a manually curated set of histone sequences grouped into 30 different variant subsets with variant-specific annotations. The curated set is supplemented by an automatically extracted set of histone sequences from the non-redundant protein database using algorithms trained on the curated set. The interactive web site supports various searching strategies in both datasets: browsing of phylogenetic trees; on-demand generation of multiple sequence alignments with feature annotations; classification of histone-like sequences and browsing of the taxonomic diversity for every histone variant. HistoneDB 2.0 is a resource for the interactive comparative analysis of histone protein sequences and their implications for chromatin function.

          Database URL: http://www.ncbi.nlm.nih.gov/projects/HistoneDB2.0

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          Most cited references20

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          Chromatin structure: a repeating unit of histones and DNA.

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            Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail.

            The canonical histone proteins are encoded by replication-dependent genes and must rapidly reach high levels of expression during S phase. In metazoans the genes that encode these proteins produce mRNAs that, instead of being polyadenylated, contain a unique 3' end structure. By contrast, the synthesis of the variant, replication-independent histones, which are encoded by polyadenylated mRNAs, persists outside of S phase. Accurate positioning of both histone types in chromatin is essential for proper transcriptional regulation, the demarcation of heterochromatic boundaries and the epigenetic inheritance of gene expression patterns. Recent results suggest that the coordinated synthesis of replication-dependent and variant histone mRNAs is achieved by signals that affect formation of the 3' end of the replication-dependent histone mRNAs.
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              Phylogenomics of the nucleosome.

              Histones are best known as the architectural proteins that package the DNA of eukaryotic organisms, forming octameric nucleosome cores that the double helix wraps tightly around. Although histones have traditionally been viewed as slowly evolving scaffold proteins that lack diversification beyond their abundant tail modifications, recent studies have revealed that variant histones have evolved for diverse functions. H2A and H3 variants have diversified to assume roles in epigenetic silencing, gene expression and centromere function. Such diversification of histone variants and 'deviants' contradicts the perception of histones as monotonous members of multigene families that indiscriminately package and compact the genome. How these diverse functions have evolved from ancestral forms can be addressed by applying phylogenetic tools to increasingly abundant sequence data.
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                Author and article information

                Journal
                Database (Oxford)
                Database (Oxford)
                databa
                databa
                Database: The Journal of Biological Databases and Curation
                Oxford University Press
                1758-0463
                2016
                17 March 2016
                17 March 2016
                : 2016
                : baw014
                Affiliations
                [1 ]National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, 8600 Rockville Pike, Bethesda, MD 20894, USA
                [2 ]Howard Hughes Medical Institute, Basic Sciences Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA
                Author notes
                *Corresponding author: Email: panch@ 123456ncbi.nlm.nih.gov , Tel: (301)435-5891; Fax: (301)480-4559 Correspondence may also be addressed to David Landsman. Email: landsman@ 123456ncbi.nlm.nih.gov
                [†]

                These authors contributed equally to this work.

                Citation details: Draizen,E.J., Shaytan,A.K., Mariño-Ramírez,L. et al. HistoneDB 2.0: a histone database with variants—an integrated resource to explore histones and their variants. Database (2016) Vol. 2016: article ID baw014; doi:10.1093/database/baw014

                Article
                baw014
                10.1093/database/baw014
                4795928
                26989147
                27a1b62f-933c-4929-93fe-5e39b17d90da
                Published by Oxford University Press 2015. This work is written by US Government employees and is in the public domain in the United States.
                History
                : 29 September 2015
                : 15 January 2016
                : 01 February 2016
                Page count
                Pages: 10
                Categories
                Original Article

                Bioinformatics & Computational biology
                Bioinformatics & Computational biology

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