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1. Full Text Regulation of the Stability of the Histone H2A-H2B Dimer by H2A Tyr57 Phosphorylation
by Sueoka, Takuma and Hayashi, Gosuke and Okamoto, Akimitsu
Biochemistry, ISSN 0006-2960, 09/2017, Volume 56, Issue 36, pp. 4767 - 4772
Histone H2A and H2B form a H2A-H2B heterodimer, which is a fundamental unit of nucleosome assembly and disassembly. Several posttranslational modifications... 
NUCLEOSOME STRUCTURE | DNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | NATIVE CHEMICAL LIGATION | GENERATION | PROTEINS | PRECURSORS | H2A/H2B DIMER | DNA - chemistry | Phosphorylation | Histones - chemistry | Models, Molecular | Protein Conformation | Protein Stability | Dimerization | Protein Folding
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2. Full Text Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification
by Tessarz, Peter and Santos-Rosa, Helena and Robson, Sam C and Sylvestersen, Kathrine B and Nelson, Christopher J and Nielsen, Michael L and Kouzarides, Tony
Nature, ISSN 0028-0836, 2014, Volume 505, Issue 7484, pp. 564 - 568
Nucleosomes are decorated with numerous post-translational modifications capable of influencing many DNA processes(1). Here we describe a new class of histone... 
NUCLEOLAR PROTEIN | DEFECTS | YFACT | VERSATILE | ROLES | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTION | COMPLEXES | FIBRILLARIN | SPT16 | ASSOCIATION | Molecular Chaperones - metabolism | Histones - chemistry | Saccharomyces cerevisiae - genetics | Humans | Methyltransferases - metabolism | Glutamine - metabolism | Molecular Sequence Data | Substrate Specificity | RNA Polymerase I - metabolism | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | Alanine - genetics | Cell Nucleolus - metabolism | Transcription, Genetic | Binding Sites | DNA, Ribosomal - genetics | RNA - metabolism | Amino Acid Sequence | Chromosomal Proteins, Non-Histone - metabolism | Nucleosomes - metabolism | Alanine - metabolism | Nuclear Proteins - metabolism | Amino Acid Motifs | Epistasis, Genetic | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Protein Processing, Post-Translational | Histones - metabolism | Methylation | Chromatin - genetics | Ribonucleoproteins, Small Nucleolar - metabolism | Physiological aspects | Covalent modifications | Research | Methyltransferases | Glutamine metabolism | Proteins | Enzymes | Cell culture | Peptides | Ribosomal DNA | DNA methylation | Genomes | Deoxyribonucleic acid--DNA
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3. Full Text RNF168 Ubiquitinates K13-15 on H2A/H2AX to Drive DNA Damage Signaling
by Mattiroli, Francesca and Vissers, Joseph H.A and van Dijk, Willem J and Ikpa, Pauline and Citterio, Elisabetta and Vermeulen, Wim and Marteijn, Jurgen A and Sixma, Titia K
Cell, ISSN 0092-8674, 09/2012, Volume 150, Issue 6, pp. 1182 - 1195
Ubiquitin-dependent signaling during the DNA damage response (DDR) to double-strand breaks (DSBs) is initiated by two E3 ligases, RNF8 and RNF168, targeting... 
X-RAY SOLUTION | RING-RING COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | SOLUTION SCATTERING | DOUBLE-STRAND BREAKS | POLYUBIQUITIN CHAINS | HOMOLOGOUS RECOMBINATION | LIGASE COMPLEX | HISTONE UBIQUITYLATION | DEPENDENT MONOUBIQUITYLATION | H2A UBIQUITINATION | CELL BIOLOGY | Protein Structure, Tertiary | Amino Acid Sequence | Histones - chemistry | Nucleosomes - chemistry | Humans | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Molecular Sequence Data | Nucleosomes - metabolism | Scattering, Small Angle | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | DNA-Binding Proteins - metabolism | X-Ray Diffraction | Lysine - metabolism | Histones - metabolism | Ubiquitin | Histones | DNA binding proteins | Ligases | DNA damage | DNA
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4. Full Text Constitutive expression exposes functional redundancy between the Arabidopsis histone H2A gene HTA1 and other H2A gene family members
by Yi, HoChul and Sardesai, Nagesh and Fujinuma, Toshinori and Chan, Chien-Wei and Veena, Veena and Gelvin, Stanton B
Plant Cell, ISSN 1040-4651, 07/2006, Volume 18, Issue 7, pp. 1575 - 1589
The Arabidopsis thaliana histone H2A gene HTA1 is essential for efficient transformation of Arabidopsis roots by Agrobacterium tumefaciens. Disruption of this... 
METHYLATION | DROSOPHILA-MELANOGASTER | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | DOUBLE-STRAND BREAKS | SACCHAROMYCES-CEREVISIAE | VARIANT | PLANT SCIENCES | CELL BIOLOGY | AGROBACTERIUM | SHOOT APEX | CELL-SPECIFIC EXPRESSION | H3 GENES | Transformation, Genetic | Amino Acid Sequence | Promoter Regions, Genetic | Arabidopsis Proteins - genetics | Multigene Family | Histones - classification | Caulimovirus - genetics | Agrobacterium tumefaciens - genetics | Molecular Sequence Data | Plant Roots - cytology | Phylogeny | Plant Roots - microbiology | Recombinant Fusion Proteins - metabolism | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Plant Roots - physiology | Sequence Alignment | Histones - genetics | Agrobacterium tumefaciens - metabolism | Gene Expression Regulation, Plant | Recombinant Fusion Proteins - genetics | Histones - metabolism | Arabidopsis Proteins - classification | Plant proteins | Genetic aspects | Research | Gene expression | Arabidopsis
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5. Full Text Structural basis of histone H2A-H2B recognition by the essential chaperone FACT
by Hondele, Maria and Stuwe, Tobias and Hassler, Markus and Halbach, Felix and Bowman, Andrew and Zhang, Elisa T and Nijmeijer, Bianca and Kotthoff, Christiane and Rybin, Vladimir and Amlacher, Stefan and Hurt, Ed and Ladurner, Andreas G
Nature, ISSN 0028-0836, 2013, Volume 499, Issue 7456, pp. 111 - 114
Facilitates chromatin transcription (FACT) is a conserved histone chaperone that reorganizes nucleosomes and ensures chromatin integrity during DNA... 
DOMAIN | COMPLEX | REPLICATION | INITIATION | TRANSCRIPT ELONGATION | DNA | MULTIDISCIPLINARY SCIENCES | SPT16 | HETERODIMER | BINDING | REVEALS | Fungal Proteins - chemistry | Protein Structure, Tertiary | Chaetomium - chemistry | Molecular Chaperones - metabolism | Protein Structure, Secondary | Histones - chemistry | Nucleosomes - chemistry | Protein Multimerization | Models, Molecular | Nucleosomes - metabolism | Substrate Specificity | Crystallography, X-Ray | DNA Replication | DNA - metabolism | Molecular Chaperones - chemistry | Amino Acid Motifs | DNA - chemistry | Conserved Sequence | Hydrophobic and Hydrophilic Interactions | Protein Binding | Histones - metabolism | Fungal Proteins - metabolism | Histones | Genetic transcription | Research | Molecular chaperones | Structure | Proteins | Mutation | Binding sites | Deoxyribonucleic acid--DNA
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6. Full Text Histone h2a monoubiquitination promotes histone h3 methylation in polycomb repression
by Kalb, R and Latwiel, S and Baymaz, H.I and Jansen, P. W and Muller, C.W and Vermeulen, M and Muller, J
Nature Structural & Molecular Biology, ISSN 1545-9993, 2014, Volume 21, Issue 6, pp. 569 - 571
A key step in gene repression by Polycomb is trimethylation of histone H3 K27 by PCR2 to form H3K27me3. H3K27me3 provides a binding surface for PRC1. We show... 
UBIQUITINATION | COMPLEX | BIOPHYSICS | PRC2 | CHROMATIN | METHYLTRANSFERASES | BIOCHEMISTRY & MOLECULAR BIOLOGY | TARGETS | JARID2 | EXPRESSION | CELL BIOLOGY | Ubiquitination | Animals | Epigenetic Repression | Polycomb-Group Proteins - genetics | Histones - metabolism | Methylation | Drosophila - genetics | Histones | Genetic research | Genetic aspects | Research | Properties | Ubiquitin-proteasome system | Gene expression | Proteins | DNA methylation | Binding sites
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7. Full Text Structural evidence for Nap1‐dependent H2A–H2B deposition and nucleosome assembly
by Aguilar‐Gurrieri, Carmen and Larabi, Amédé and Vinayachandran, Vinesh and Patel, Nisha A and Yen, Kuangyu and Reja, Rohit and Ebong, Ima‐O and Schoehn, Guy and Robinson, Carol V and Pugh, B Franklin and Panne, Daniel
The EMBO Journal, ISSN 0261-4189, 07/2016, Volume 35, Issue 13, pp. 1465 - 1482
Nap1 is a histone chaperone involved in the nuclear import of H2A–H2B and nucleosome assembly. Here, we report the crystal structure of Nap1 bound to H2A–H2B... 
H2A–H2B | Nap1 | nucleosome assembly | chromatin | histone chaperone | Histone chaperone | Chromatin | Nucleosome assembly | H2A-H2B | STRUCTURE REFINEMENT | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ELECTRON-MICROSCOPY | RECOMBINANT HISTONES | MAMMALIAN-CELLS | CELL BIOLOGY | ANGSTROM RESOLUTION | IN-VITRO | PROTEIN-1 | HISTONE CHAPERONE NAP1 | CORE PARTICLE | Nucleosome Assembly Protein 1 - genetics | Nucleosome Assembly Protein 1 - metabolism | Histones - chemistry | Protein Multimerization | Models, Molecular | Nucleosomes - metabolism | Crystallography, X-Ray | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - chemistry | Saccharomyces cerevisiae - metabolism | Nucleosome Assembly Protein 1 - chemistry | Chromatin Immunoprecipitation | DNA Mutational Analysis | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Conformation | Histones - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Eukaryotes | Molecular biology | Crystal structure | Life Sciences | Biomolecules | Biochemistry, Molecular Biology | Chromatin, Epigenetics, Genomics & Functional Genomics | Structural Biology
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8. Full Text Transcriptional repression by PRC1 in the absence of H2A monoubiquitylation
by Pengelly, Ana Raquel and Kalb, Reinhard and Finkl, Katja and Müller, Jürg
Genes and Development, ISSN 0890-9369, 07/2015, Volume 29, Issue 14, pp. 1487 - 1492
Histone H2A monoubiquitylation (H2Aub) is considered to be a key effector in transcriptional repression by Polycomb-repressive complex 1 (PRC1). We analyzed... 
H2A and H2Av monoubiquitylation | Polycomb | PRC1 | Drosophila | Transcriptional repression | X-INACTIVATION | DOMAIN | HISTONE H2A | CHROMATIN-STRUCTURE | DEVELOPMENTAL BIOLOGY | CELL BIOLOGY | UBIQUITIN LIGASE COMPLEX | transcriptional repression | POLYCOMB REPRESSION | IN-VIVO | RING1B | GENETICS & HEREDITY | UBIQUITYLATION | PROTEINS | Polycomb Repressive Complex 1 - metabolism | Ubiquitin-Protein Ligases - metabolism | Gene Expression Regulation, Developmental - genetics | Drosophila Proteins - metabolism | Polycomb Repressive Complex 1 - genetics | Ubiquitination | Animals | Histones - genetics | Metamorphosis, Biological - genetics | Drosophila - embryology | Drosophila Proteins - genetics | Histones - metabolism | Mutation | Drosophila - genetics | Histones | Genetic transcription | Research | Ubiquitin-proteasome system | Mutation (Biology) | Research Communication
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9. Full Text Nucleotide Excision Repair-Induced H2A Ubiquitination Is Dependent on MDC1 and RNF8 and Reveals a Universal DNA Damage Response
by Jurgen A. Marteijn and Simon Bekker-Jensen and Niels Mailand and Hannes Lans and Petra Schwertman and Audrey M. Gourdin and Nico P. Dantuma and Jiri Lukas and Wim Vermeulen
The Journal of Cell Biology, ISSN 0021-9525, 9/2009, Volume 186, Issue 6, pp. 835 - 847
Chromatin modifications are an important component of the of DNA damage response (DDR) network that safeguard genomic integrity. Recently, we demonstrated... 
Chromatin | DNA damage | DNA | Cell lines | Cephalopelvic disproportion | HeLa cells | Histones | Cellular immunity | Lesions | DNA repair | UV-IRRADIATION | CHROMATIN | PROTEASOMAL DEGRADATION | PHOSPHORYLATION | PROTEIN XPC | IN-VIVO | DOUBLE-STRAND BREAKS | HISTONE H2AX | CHECKPOINT | ATR | CELL BIOLOGY | Epigenesis, Genetic | Humans | Intracellular Signaling Peptides and Proteins - metabolism | DNA - radiation effects | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - deficiency | DNA-Binding Proteins - metabolism | Ubiquitination | Transfection | Ultraviolet Rays | RNA Interference | Time Factors | BRCA1 Protein - metabolism | Trans-Activators - genetics | Signal Transduction - radiation effects | Nuclear Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Cell Cycle Proteins - metabolism | Nuclear Proteins - metabolism | Ataxia Telangiectasia Mutated Proteins | DNA-Binding Proteins - genetics | Ubiquitin-Conjugating Enzymes - metabolism | DNA Repair | Trans-Activators - metabolism | Protein Processing, Post-Translational | DNA Damage | HeLa Cells | Histones - metabolism | Tumor Suppressor p53-Binding Protein 1 | Dose-Response Relationship, Radiation | Physiological aspects | Genetic aspects | Research | Ubiquitin-proteasome system | Proteins | Enzymes | Genomics | Deoxyribonucleic acid--DNA | Index Medicus
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10. Full Text Demethylation of H3K27 Regulates Polycomb Recruitment and H2A Ubiquitination
by Min Gyu Lee and Raffaella Villa and Patrick Trojer and Jessica Norman and Kai-Ping Yan and Danny Reinberg and Luciano Di Croce and Ramin Shiekhattar
Science, ISSN 0036-8075, 10/2007, Volume 318, Issue 5849, pp. 447 - 450
Methylation of histone H3 lysine 27 (H3K27) is a posttranslational modification that is highly correlated with genomic silencing. Here we show that human UTX,... 
Transcriptional regulatory elements | HEK293 cells | Genes | Cell lines | Histones | Small interfering RNA | Antibodies | Reports | Gene expression regulation | Repression | Methylation | TRIMETHYLATION | HISTONE LYSINE METHYLATION | TARGET GENES | COMPLEX | PROTEIN | MULTIDISCIPLINARY SCIENCES | METHYLTRANSFERASE ACTIVITY | ENHANCER | CELL FATE | GENOME | Multigene Family | Humans | Transcriptional Activation | Ubiquitin - metabolism | Neoplasm Proteins - metabolism | DNA-Binding Proteins - metabolism | Tretinoin - metabolism | Transcription, Genetic | Cell Differentiation | Lysine - metabolism | Nuclear Proteins - genetics | Genes, Homeobox | Repressor Proteins - metabolism | Tretinoin - pharmacology | Recombinant Proteins - metabolism | Cell Line | Promoter Regions, Genetic | Signal Transduction | Nuclear Proteins - metabolism | Polycomb-Group Proteins | Histone Demethylases | Cell Line, Tumor | Protein Processing, Post-Translational | Embryonic Stem Cells | Histones - metabolism | Gene silencing | Genetic aspects | Chemical properties | Research | Proteins | Signal transduction | Biochemistry | Genomics
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11. Full Text Variant PRC1 Complex-Dependent H2A Ubiquitylation Drives PRC2 Recruitment and Polycomb Domain Formation
by Blackledge, Neil P and Farcas, Anca M and Kondo, Kaori and Kondo, Takashi and King, Hamish W and McGouran, Joanna F and Hanssen, Lars L.P and Ito, Shinsuke and Cooper, Sarah and Koseki, Haruhiko and Koseki, Yoko and Ishikura, Tomoyuki and Long, Hannah K and Sheahan, Thomas W and Brockdorff, Neil and Kessler, Benedikt M and Klose, Robert J
Cell, ISSN 0092-8674, 06/2014, Volume 157, Issue 6, pp. 1445 - 1459
Chromatin modifying activities inherent to polycomb repressive complexes PRC1 and PRC2 play an essential role in gene regulation, cellular differentiation, and... 
HISTONE METHYLTRANSFERASE ACTIVITY | GROUP PROTEINS RING1A/B | X-INACTIVATION | REPRESSIVE COMPLEX | UBIQUITIN LIGASE COMPLEX | DROSOPHILA-MELANOGASTER | BIOCHEMISTRY & MOLECULAR BIOLOGY | EMBRYONIC STEM-CELLS | GENOME-WIDE | CPG ISLANDS | SAM DOMAIN | CELL BIOLOGY | Protein Structure, Tertiary | Embryonic Stem Cells - metabolism | Genome-Wide Association Study | F-Box Proteins - metabolism | Polycomb Repressive Complex 1 - metabolism | F-Box Proteins - chemistry | Bone Development | Jumonji Domain-Containing Histone Demethylases - genetics | Genes, Lethal | Animals | CpG Islands | Jumonji Domain-Containing Histone Demethylases - chemistry | Mice | Histones - metabolism | Polycomb Repressive Complex 2 - metabolism | F-Box Proteins - genetics | Jumonji Domain-Containing Histone Demethylases - metabolism | Ubiquitin | Chromatin | Cell differentiation | Embryonic stem cells | Proteolysis | Employee recruitment
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12. Full Text RYBP-PRC1 Complexes Mediate H2A Ubiquitylation at Polycomb Target Sites Independently of PRC2 and H3K27me3
by Tavares, Lígia and Dimitrova, Emilia and Oxley, David and Webster, Judith and Poot, Raymond and Demmers, Jeroen and Bezstarosti, Karel and Taylor, Stephen and Ura, Hiroki and Koide, Hiroshi and Wutz, Anton and Vidal, Miguel and Elderkin, Sarah and Brockdorff, Neil
Cell, ISSN 0092-8674, 02/2012, Volume 148, Issue 4, pp. 664 - 678
Polycomb-repressive complex 1 (PRC1) has a central role in the regulation of heritable gene silencing during differentiation and development. PRC1 recruitment... 
RNA-POLYMERASE-II | GROUP PROTEINS RING1A/B | X-INACTIVATION | REPRESSIVE COMPLEX | HISTONE H2A | DEVELOPMENTAL REGULATORS | CHROMATIN-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | EMBRYONIC STEM-CELLS | TRANSCRIPTION FACTOR YY1 | C-TERMINAL DOMAIN | CELL BIOLOGY | Cell Line | Embryonic Stem Cells - metabolism | Ubiquitin-Protein Ligases - metabolism | Repressor Proteins - genetics | Polycomb-Group Proteins | Polycomb Repressive Complex 2 | Ubiquitination | Animals | Polycomb Repressive Complex 1 | Mice | Histones - metabolism | Repressor Proteins - metabolism | Fibroblasts - metabolism | Ubiquitin | Stem cell research | Genes | Stem cells | Universities and colleges | Embryonic stem cells | Mass spectrometry
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