The Histone Database: an integrated resource for histones and histone fold-containing proteins

Eukaryotic chromatin is composed of DNA and protein components—core histones—that act to compactly pack the DNA into nucleosomes, the fundamental building blocks of chromatin. These nucleosomes are connected to adjacent nucleosomes by linker histones. Nucleosomes are highly dynamic and, through various core histone post-translational modifications and incorporation of diverse histone variants, can serve as epigenetic marks to control processes such as gene expression and recombination. The Histone Sequence Database is a curated collection of sequences and structures of histones and non-histone proteins containing histone folds, assembled from major public databases. Here, we report a substantial increase in the number of sequences and taxonomic coverage for histone and histone fold-containing proteins available in the database. Additionally, the database now contains an expanded dataset that includes archaeal histone sequences. The database also provides comprehensive multiple sequence alignments for each of the four core histones (H2A, H2B, H3 and H4), the linker histones (H1/H5) and the archaeal histones. The database also includes current information on solved histone fold-containing structures. The Histone Sequence Database is an inclusive resource for the analysis of chromatin structure and function focused on histones and histone fold-containing proteins. Database URL: The Histone Sequence Database is freely available and can be accessed at http://research.nhgri.nih.gov/histones/.

[1]  J. Reeve,et al.  Deletion of the archaeal histone in Methanosarcina mazei Gö1 results in reduced growth and genomic transcription , 2008, Molecular microbiology.

[2]  Makoto Inoue,et al.  Automated system for high-throughput protein production using the dialysis cell-free method. , 2009, Protein expression and purification.

[3]  J. Ausió,et al.  Bmc Evolutionary Biology the Evolutionary Differentiation of Two Histone H2a.z Variants in Chordates (h2a.z-1 and H2a.z-2) Is Mediated by a Stepwise Mutation Process That Affects Three Amino Acid Residues , 2022 .

[4]  Peng-Fei Xu,et al.  Genome-Wide Survey and Developmental Expression Mapping of Zebrafish SET Domain-Containing Genes , 2008, PloS one.

[5]  T. Richmond,et al.  Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution. , 2002, Journal of molecular biology.

[6]  Robert S. Ledley,et al.  The Protein Information Resource , 2003, Nucleic Acids Res..

[7]  S Henikoff,et al.  Epigenetic inheritance of centromeres. , 2010, Cold Spring Harbor symposia on quantitative biology.

[8]  B. Wang,et al.  The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[9]  Robert C. Edgar,et al.  MUSCLE: multiple sequence alignment with high accuracy and high throughput. , 2004, Nucleic acids research.

[10]  C. Allis,et al.  New functions for an old variant: no substitute for histone H3.3. , 2010, Current opinion in genetics & development.

[11]  Linda Hanley-Bowdoin,et al.  Genome-Wide Analysis of the Core DNA Replication Machinery in the Higher Plants Arabidopsis and Rice1[W][OA] , 2007, Plant Physiology.

[12]  Johannes Söding,et al.  On the origin of the histone fold , 2007, BMC Structural Biology.

[13]  J A Lake,et al.  An ancestral nuclear protein assembly: Crystal structure of the Methanopyrus kandleri histone , 2001, Protein science : a publication of the Protein Society.

[14]  Kairong Cui,et al.  H3.3/H2A.Z double variant-containing nucleosomes mark ‘nucleosome-free regions’ of active promoters and other regulatory regions in the human genome , 2009, Nature Genetics.

[15]  T. Richmond,et al.  Crystal structure of the nucleosome core particle at 2.8 Å resolution , 1997, Nature.

[16]  S. Khochbin,et al.  Histone H1 diversity: bridging regulatory signals to linker histone function. , 2001, Gene.

[17]  Benjamin A. Shoemaker,et al.  Histone structure and nucleosome stability , 2005, Expert review of proteomics.

[18]  Ronald W. Davis,et al.  A genome-wide transcriptional analysis of the mitotic cell cycle. , 1998, Molecular cell.

[19]  D. Landsman,et al.  Multiple independent evolutionary solutions to core histone gene regulation , 2006, Genome Biology.

[20]  T. Eickbush,et al.  The histone core complex: an octamer assembled by two sets of protein-protein interactions. , 1978, Biochemistry.

[21]  N. Sharma,et al.  Nucleosome eviction and activated transcription require p300 acetylation of histone H3 lysine 14 , 2010, Proceedings of the National Academy of Sciences.

[22]  Benjamin J. Hsu,et al.  The histone database: A comprehensive resource for histones and histone fold‐containing proteins , 2005, Proteins.

[23]  J F Gibrat,et al.  Surprising similarities in structure comparison. , 1996, Current opinion in structural biology.

[24]  Dustin E. Schones,et al.  Genome-wide approaches to studying chromatin modifications , 2008, Nature Reviews Genetics.

[25]  J. Dacks,et al.  Origin of H1 linker histones , 2001, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[26]  Ahsan Huda,et al.  Epigenetic histone modifications of human transposable elements: genome defense versus exaptation , 2010, Mobile DNA.

[27]  Sean R Eddy,et al.  A new generation of homology search tools based on probabilistic inference. , 2009, Genome informatics. International Conference on Genome Informatics.

[28]  W. Delano The PyMOL Molecular Graphics System , 2002 .

[29]  S. Bryant,et al.  Threading a database of protein cores , 1995, Proteins.

[30]  Steven Henikoff,et al.  Histone variants — ancient wrap artists of the epigenome , 2010, Nature Reviews Molecular Cell Biology.

[31]  Michael Bustin,et al.  The dynamics of histone H1 function in chromatin. , 2005, Molecular cell.

[32]  J. Ausió,et al.  Birth-and-death long-term evolution promotes histone H2B variant diversification in the male germinal cell line. , 2010, Molecular biology and evolution.

[33]  Youngchang Kim,et al.  The crystal structure of Aq_328 from the hyperthermophilic bacteria Aquifex aeolicus shows an ancestral histone fold , 2005, Proteins.

[34]  Davit A Potoyan,et al.  Energy landscape analyses of disordered histone tails reveal special organization of their conformational dynamics. , 2011, Journal of the American Chemical Society.

[35]  Corinna Kolárik,et al.  Identification of histone modifications in biomedical text for supporting epigenomic research , 2009, BMC Bioinformatics.

[36]  J. Reeve,et al.  Archaeal histones and the origin of the histone fold. , 2006, Current opinion in microbiology.

[37]  E. Lundberg,et al.  A Genecentric Human Protein Atlas for Expression Profiles Based on Antibodies* , 2008, Molecular & Cellular Proteomics.

[38]  Holger Sondermann,et al.  Tandem histone folds in the structure of the N-terminal segment of the ras activator Son of Sevenless. , 2003, Structure.

[39]  Yanli Wang,et al.  MMDB: annotating protein sequences with Entrez's 3D-structure database , 2006, Nucleic Acids Res..

[40]  Steven Henikoff,et al.  Phylogenomics of the nucleosome , 2003, Nature Structural Biology.

[41]  D. Landsman,et al.  A variety of DNA-binding and multimeric proteins contain the histone fold motif. , 1995, Nucleic acids research.

[42]  J. Ausió,et al.  Histone variants--the structure behind the function. , 2006, Briefings in functional genomics & proteomics.

[43]  T. Kouzarides Chromatin Modifications and Their Function , 2007, Cell.

[44]  David L. Wheeler,et al.  GenBank , 2015, Nucleic Acids Res..

[45]  Ozlem Keskin,et al.  Molecular Recognition of H3/H4 Histone Tails by the Tudor Domains of JMJD2A: A Comparative Molecular Dynamics Simulations Study , 2011, PloS one.

[46]  T. N. Bhat,et al.  The Protein Data Bank , 2000, Nucleic Acids Res..