Histone Chaperones: Proteins involved in the assembly and disassembly of HISTONES into NUCLEOSOMES.Molecular Chaperones: A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.Histones: Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each.Nucleosome Assembly Protein 1: A histone chaperone that facilitates nucleosome assembly by mediating the formation of the histone octamer and its transfer to DNA.Nucleosomes: The repeating structural units of chromatin, each consisting of approximately 200 base pairs of DNA wound around a protein core. This core is composed of the histones H2A, H2B, H3, and H4.Chromatin Assembly and Disassembly: The mechanisms effecting establishment, maintenance, and modification of that specific physical conformation of CHROMATIN determining the transcriptional accessibility or inaccessibility of the DNA.Acetylation: Formation of an acetyl derivative. (Stedman, 25th ed)Histone Deacetylases: Deacetylases that remove N-acetyl groups from amino side chains of the amino acids of HISTONES. The enzyme family can be divided into at least three structurally-defined subclasses. Class I and class II deacetylases utilize a zinc-dependent mechanism. The sirtuin histone deacetylases belong to class III and are NAD-dependent enzymes.Chromatin Assembly Factor-1: A histone chaperone protein that plays a role in the deposition of NUCLEOSOMES on newly synthesized DNA. It is comprised of three different subunits of 48, 60, and 150 kDa molecular size. The 48 kDa subunit, RETINOBLASTOMA-BINDING PROTEIN 4, is also a component of several other protein complexes involved in chromatin remodeling.Histone Acetyltransferases: Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.Chromatin: The material of CHROMOSOMES. It is a complex of DNA; HISTONES; and nonhistone proteins (CHROMOSOMAL PROTEINS, NON-HISTONE) found within the nucleus of a cell.Nucleoplasmins: A family of histone molecular chaperones that play roles in sperm CHROMATIN decondensation and CHROMATIN ASSEMBLY in fertilized eggs. They were originally discovered in XENOPUS egg extracts as histone-binding factors that mediate nucleosome formation in vitro.Retinoblastoma-Binding Protein 4: A retinoblastoma-binding protein that is involved in CHROMATIN REMODELING, histone deacetylation, and repression of GENETIC TRANSCRIPTION. Although initially discovered as a retinoblastoma binding protein it has an affinity for core HISTONES and is a subunit of chromatin assembly factor-1 and polycomb repressive complex 2.Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.Cell Cycle Proteins: Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.Chromosomal Proteins, Non-Histone: Nucleoproteins, which in contrast to HISTONES, are acid insoluble. They are involved in chromosomal functions; e.g. they bind selectively to DNA, stimulate transcription resulting in tissue-specific RNA synthesis and undergo specific changes in response to various hormones or phytomitogens.Transcriptional Elongation Factors: Transcription factors whose primary function is to regulate the rate in which RNA is transcribed.Histone Deacetylase Inhibitors: Compounds that inhibit HISTONE DEACETYLASES. This class of drugs may influence gene expression by increasing the level of acetylated HISTONES in specific CHROMATIN domains.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Nuclear Proteins: Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Retinoblastoma-Binding Protein 7: A retinoblastoma-binding protein that has an affinity for core HISTONES. It is found as a subunit of protein complexes that are in involved in the enzymatic modification of histones including the Mi2 and Sin3 histone deacetylase complexes and the polycomb repressive complex 2.Gene Silencing: Interruption or suppression of the expression of a gene at transcriptional or translational levels.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.Methylation: Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed)HSP70 Heat-Shock Proteins: A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.High Mobility Group Proteins: A family of low-molecular weight, non-histone proteins found in chromatin.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Gene Expression Regulation, Fungal: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in fungi.HeLa Cells: The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.Histone Deacetylase 1: A histone deacetylase subtype that is found along with HISTONE DEACETYLASE 2; RETINOBLASTOMA-BINDING PROTEIN 4; and RETINOBLASTOMA-BINDING PROTEIN 7 as core components of histone deacetylase complexes.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Epigenesis, Genetic: A genetic process by which the adult organism is realized via mechanisms that lead to the restriction in the possible fates of cells, eventually leading to their differentiated state. Mechanisms involved cause heritable changes to cells without changes to DNA sequence such as DNA METHYLATION; HISTONE modification; DNA REPLICATION TIMING; NUCLEOSOME positioning; and heterochromatization which result in selective gene expression or repression.HSP90 Heat-Shock Proteins: A class of MOLECULAR CHAPERONES whose members act in the mechanism of SIGNAL TRANSDUCTION by STEROID RECEPTORS.DNA-Binding Proteins: Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.HSP40 Heat-Shock Proteins: A family of heat-shock proteins that contain a 70 amino-acid consensus sequence known as the J domain. The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins.Protein Interaction Domains and Motifs: Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS.Histone Code: The specific patterns of changes made to HISTONES, that are involved in assembly, maintenance, and alteration of chromatin structural states (such as EUCHROMATIN and HETEROCHROMATIN). The changes are made by various HISTONE MODIFICATION PROCESSES that include ACETYLATION; METHYLATION; PHOSPHORYLATION; and UBIQUITINATION.Heat-Shock Proteins: Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions.Histone Deacetylase 2: A histone deacetylase subtype that is found along with HISTONE DEACETYLASE 1; RETINOBLASTOMA-BINDING PROTEIN 4; and RETINOBLASTOMA-BINDING PROTEIN 7 as core components of histone deacetylase complexes.Heterochromatin: The portion of chromosome material that remains condensed and is transcriptionally inactive during INTERPHASE.Histone Demethylases: Enzymes that catalyse the removal of methyl groups from LYSINE or ARGININE residues found on HISTONES. Many histone demethylases generally function through an oxidoreductive mechanism.DNA Replication: The process by which a DNA molecule is duplicated.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Hydroxamic Acids: A class of weak acids with the general formula R-CONHOH.Telomere Homeostasis: Maintenance of TELOMERE length. During DNA REPLICATION, chromosome ends loose some of their telomere sequence (TELOMERE SHORTENING.) Various cellular mechanism are involved in repairing, extending, and recapping the telomere ends.Multiprotein Complexes: Macromolecular complexes formed from the association of defined protein subunits.Histone-Lysine N-Methyltransferase: An enzyme that catalyzes the methylation of the epsilon-amino group of lysine residues in proteins to yield epsilon mono-, di-, and trimethyllysine. EC 2.1.1.43.RNA Polymerase II: A DNA-dependent RNA polymerase present in bacterial, plant, and animal cells. It functions in the nucleoplasmic structure and transcribes DNA into RNA. It has different requirements for cations and salt than RNA polymerase I and is strongly inhibited by alpha-amanitin. EC 2.7.7.6.Chromatin Immunoprecipitation: A technique for identifying specific DNA sequences that are bound, in vivo, to proteins of interest. It involves formaldehyde fixation of CHROMATIN to crosslink the DNA-BINDING PROTEINS to the DNA. After shearing the DNA into small fragments, specific DNA-protein complexes are isolated by immunoprecipitation with protein-specific ANTIBODIES. Then, the DNA isolated from the complex can be identified by PCR amplification and sequencing.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.Drosophila Proteins: Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.Repressor Proteins: Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Adenosine Triphosphatases: A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.Cell Line: Established cell cultures that have the potential to propagate indefinitely.DNA Damage: Injuries to DNA that introduce deviations from its normal, intact structure and which may, if left unrepaired, result in a MUTATION or a block of DNA REPLICATION. These deviations may be caused by physical or chemical agents and occur by natural or unnatural, introduced circumstances. They include the introduction of illegitimate bases during replication or by deamination or other modification of bases; the loss of a base from the DNA backbone leaving an abasic site; single-strand breaks; double strand breaks; and intrastrand (PYRIMIDINE DIMERS) or interstrand crosslinking. Damage can often be repaired (DNA REPAIR). If the damage is extensive, it can induce APOPTOSIS.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)S Phase: Phase of the CELL CYCLE following G1 and preceding G2 when the entire DNA content of the nucleus is replicated. It is achieved by bidirectional replication at multiple sites along each chromosome.Protein Multimerization: The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.Schizosaccharomyces pombe Proteins: Proteins obtained from the species Schizosaccharomyces pombe. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.Schizosaccharomyces: A genus of ascomycetous fungi of the family Schizosaccharomycetaceae, order Schizosaccharomycetales.Gene Expression Regulation: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.Protein Transport: The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.Lysine: An essential amino acid. It is often added to animal feed.Chaperonins: A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences.Genomic Instability: An increased tendency of the GENOME to acquire MUTATIONS when various processes involved in maintaining and replicating the genome are dysfunctional.Protein Interaction Mapping: Methods for determining interaction between PROTEINS.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.Calnexin: A lectin found in ENDOPLASMIC RETICULUM membranes that binds to specific N-linked OLIGOSACCHARIDES found on newly synthesized proteins. It may play role in PROTEIN FOLDING or retention and degradation of misfolded proteins in the endoplasmic reticulum.DNA Repair: The reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule which contained damaged regions. The major repair mechanisms are excision repair, in which defective regions in one strand are excised and resynthesized using the complementary base pairing information in the intact strand; photoreactivation repair, in which the lethal and mutagenic effects of ultraviolet light are eliminated; and post-replication repair, in which the primary lesions are not repaired, but the gaps in one daughter duplex are filled in by incorporation of portions of the other (undamaged) daughter duplex. Excision repair and post-replication repair are sometimes referred to as "dark repair" because they do not require light.Cell Cycle: The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.Gene Deletion: A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.Recombinant Proteins: Proteins prepared by recombinant DNA technology.HSC70 Heat-Shock Proteins: A constitutively expressed subfamily of the HSP70 heat-shock proteins. They preferentially bind and release hydrophobic peptides by an ATP-dependent process and are involved in post-translational PROTEIN TRANSLOCATION.Jumonji Domain-Containing Histone Demethylases: A family of histone demethylases that share a conserved Jumonji C domain. The enzymes function via an iron-dependent dioxygenase mechanism that couples the conversion of 2-oxoglutarate to succinate to the hydroxylation of N-methyl groups.Autoantigens: Endogenous tissue constituents that have the ability to interact with AUTOANTIBODIES and cause an immune response.Xenopus laevis: The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.Drosophila melanogaster: A species of fruit fly much used in genetics because of the large size of its chromosomes.Transcriptional Activation: Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.Promoter Regions, Genetic: DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.Telomere: A terminal section of a chromosome which has a specialized structure and which is involved in chromosomal replication and stability. Its length is believed to be a few hundred base pairs.Acetyltransferases: Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Endoplasmic Reticulum: A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)Ribonucleases: Enzymes that catalyze the hydrolysis of ester bonds within RNA. EC 3.1.-.Protein Methyltransferases: Enzymes that catalyze the methylation of amino acids after their incorporation into a polypeptide chain. S-Adenosyl-L-methionine acts as the methylating agent. EC 2.1.1.Calreticulin: A multifunctional protein that is found primarily within membrane-bound organelles. In the ENDOPLASMIC RETICULUM it binds to specific N-linked oligosaccharides found on newly-synthesized proteins and functions as a MOLECULAR CHAPERONE that may play a role in PROTEIN FOLDING or retention and degradation of misfolded proteins. In addition calreticulin is a major storage form for CALCIUM and functions as a calcium-signaling molecule that can regulate intracellular calcium HOMEOSTASIS.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Drosophila: A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.p300-CBP Transcription Factors: A family of histone acetyltransferases that is structurally-related to CREB-BINDING PROTEIN and to E1A-ASSOCIATED P300 PROTEIN. They function as transcriptional coactivators by bridging between DNA-binding TRANSCRIPTION FACTORS and the basal transcription machinery. They also modify transcription factors and CHROMATIN through ACETYLATION.Lactams, Macrocyclic: LACTAMS forming compounds with a ring size of approximately 1-3 dozen atoms.Cell Nucleus: Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)Chaperonin 60: A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.Benzoquinones: Benzene rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
Histone chaperone • Chromatin remodeling factor • Histone acetyltransferase • Histone deacetyltransferase • DNA ... Milutinovic S, Zhuang Q, Szyf M (June 2002). "Proliferating cell nuclear antigen associates with histone deacetylase activity, ...
"Histone chaperone networks shaping chromatin function". Nature Reviews Molecular Cell Biology. 18 (3): 141-158. doi:10.1038/nrm ... by homology to eukaryotic histones, and in the case of bacteria, by histone-like proteins. Bacterial chromosomes tend to be ... histone proteins Each chromatin fibre consists of one DNA helix coiled around eight histone molecules like a loop; such a ... This structure is, however, dynamic and is maintained and remodeled by the actions of a range of histone-like proteins, which ...
JDP2 displays histone-binding and histone-chaperone activity. and inhibition of p300/CBP induced histone acetylation (INHAT). ... Huang YC, Saito S, Yokoyama KK (Oct 2010). "Histone chaperone Jun dimerization protein 2 (JDP2): role in cellular senescence ... The histone-binding region is located from position 35 to 72 and the inhibition of the histone acetyltransferase (INHAT) region ... JDP2 recruits histone deacetylases HDAC1 and HDAC2, HDAC6 and HDAC3. JDP2 has INHAT activity and inhibits histone methylation ...
... and p50 subunits that assembles histone tetramers onto replicating DNA in vitro This complex is histone chaperone involved in ... "The Cac1 subunit of histone chaperone CAF-1 organizes CAF-1-H3/H4 architecture and tetramerizes histones". ELife. 5: e18023. ... 2015). "The histone chaperone CAF-1 safeguards somatic cell identity". Nature. 528 (7581): 218-224. doi:10.1038/nature15749. ... ScienceDaily Yu Z, Liu J, Deng WM, Jiao R (2015). "Histone chaperone CAF-1: essential roles in multi-cellular organism ...
Another histone chaperone that associates with the replisome is Asf1, which interacts with the Mcm complex dependent on histone ... There are several histone chaperones that are known to be involved in nucleosome assembly after replication. The FACT complex ... Huang S, Zhou H, Katzmann D, Hochstrasser M, Atanasova E, Zhang Z (September 2005). "Rtt106p is a histone chaperone involved in ... The nucleosome octamer includes two copies of each histone H2A, H2B, H3, and H4. Due to the tight association of histone ...
"ANP32E is a histone chaperone that removes H2A.Z from chromatin". Nature. 505 (7485): 648-53. doi:10.1038/nature12922. PMID ... In mammalian cells, ANP32E has been shown to be an H2A.Z chaperone capable of promoting the removal of H2A.Z from chromatin. In ...
Histone chaperone ASF1B is a protein that in humans is encoded by the ASF1B gene. This gene encodes a member of the H3/H4 ... Loyola A, Almouzni G (Mar 2004). "Histone chaperones, a supporting role in the limelight". Biochimica et Biophysica Acta. 1677 ... Umehara T, Horikoshi M (Sep 2003). "Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in ... family of histone chaperone proteins and is similar to the anti-silencing function-1 gene in yeast. The encoded protein is the ...
"Automodification switches PARP-1 function from chromatin architectural protein to histone chaperone". Proc. Natl. Acad. Sci. U. ... a novel crosstalk between histone modification H3K9ac and ETS1 motif hypomethylation in BRCA1-mutated ovarian cancer". ...
... forms a complex with DAXX which is an histone H3.3 chaperone. ATRX has been also shown to interact with EZH2. Alpha- ... Lewis PW, Elsaesser SJ, Noh KM, Stadler SC, Allis CD (August 2010). "Daxx is an H3.3-specific histone chaperone and cooperates ... December 2015). "Histone variant H3.3 provides the heterochromatic H3 lysine 9 tri-methylation mark at telomeres". Nucleic ... Elsässer SJ, Noh KM, Diaz N, Allis CD, Banaszynski LA (June 2015). "Histone H3.3 is required for endogenous retroviral element ...
It can shuttle between the cytoplasm and nucleus, suggesting a role as a histone chaperone. This gene is one of several located ... Rodriguez P, Pelletier J, Price GB, Zannis-Hadjopoulos M (2000). "NAP-2: histone chaperone function and phosphorylation state ... 1997). "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone". ... family which can interact with both core and linker histones. ...
"Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights". Structure. 15 (2): ... "Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4". Nature. 446 (7133): 338-41. doi: ... Histone chaperone ASF1A is a protein that in humans is encoded by the ASF1A gene. This gene encodes a member of the H3/H4 ... Umehara T, Horikoshi M (Sep 2003). "Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in ...
2000). "A human homologue of yeast anti-silencing factor has histone chaperone activity". Genes Cells. 5 (3): 221-33. doi: ... Histone H3.1 is a protein that in humans is encoded by the HIST1H3C gene. Histones are basic nuclear proteins that are ... "Entrez Gene: HIST1H3C histone cluster 1, H3c". Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus ... Umehara T, Horikoshi M (2003). "Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in ...
2000). "A human homologue of yeast anti-silencing factor has histone chaperone activity". Genes Cells. 5 (3): 221-33. doi: ... Histone H4 is a protein that in humans is encoded by the HIST1H4F gene. Histones are basic nuclear proteins that are ... Umehara T, Horikoshi M (2003). "Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in ... "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): 940-8. ...
Daxx serves as an H3.3 specific histone chaperone, interacting with an H3.3/H4 dimer. It interacts with a wide variety of ... Lewis PW, Elsaesser SJ, Noh KM, Stadler SC, Allis CD (2010). "Daxx is an H3.3-specific histone chaperone and cooperates with ...
"Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly". Nat. Struct. Mol ... Transcription Recovery after DNA Damage Requires Chromatin Priming by the H3.3 Histone Chaperone HIRA. Cell, 155(1), 94-106. ... Lorain S, Quivy JP, Monier-Gavelle F, Scamps C, Lécluse Y, Almouzni G, Lipinski M (1998). "Core histones and HIRIP3, a novel ... Lorain S, Quivy JP, Monier-Gavelle F, Scamps C, Lécluse Y, Almouzni G, Lipinski M (September 1998). "Core histones and HIRIP3, ...
1997). "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone". ... Histone H4 is a protein that in humans is encoded by the HIST2H4A gene. Histones are basic nuclear proteins that are ... "Entrez Gene: HIST2H4A histone cluster 2, H4a". Green L, Van Antwerpen R, Stein J, et al. (1984). "A major human histone gene ... This gene is found in a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are ...
1997). "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone". ... Histone H2B type 2-E is a protein that in humans is encoded by the HIST2H2BE gene. Histones are basic nuclear proteins that are ... 1998). "Core Histones and HIRIP3, a Novel Histone-Binding Protein, Directly Interact with WD Repeat Protein HIRA". Mol. Cell. ... "Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T ...
1997). "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone". ... Histone H2A type 1-B/E is a protein that in humans is encoded by the HIST1H2AE gene. Histones are basic nuclear proteins that ... "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): 940-8. ... 2004). "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo". Genes Dev. 18 ( ...
He demonstrated the histone chaperone activity and the acetylation of chromatin transcription and these findings have been ... V Swaminathan; A Hari Kishore; KK Febitha; Tapas K Kundu (September 2005). "Human histone chaperone nucleophosmin enhances ... of histone acetyltransferases". Use of certain benzoic acid and benzamide compounds as modulators of enzymes histone ... "Inhibition of Histone Acetyltransferases by CTK7A and Mthods thereof". Method for inhibiting histone acetyltransferases by ...
Arabidopsis NRP1 and NRP2 encode histone chaperones and are required for maintaining postembryonic root growth. The Plant Cell ...
During the assembly of regular nucleosomal arrays, these nucleoplasmins transfer the DNA to them by binding to the histones. ... Dingwall, C.; Laskey, R. A. (1990). "Nucleoplasmin: the archetypal molecular chaperone". Seminars in cell biology. 1 (1). ... Nucleoplasmin, the first identified molecular chaperone is a thermostable acidic protein with a pentameric structure. The ... C, Dingwall; RA., Laskey (Feb 1990). "Nucleoplasmin: the archetypal molecular chaperone". Seminars in Cell Biology. 1 (1): 11- ...
Interestingly, although the vertebrate chaperone HJURP and the yeast chaperone Scm3 have diverged, their N-terminal domains ... Although certain histone modifications at centromeres seem to serve a purpose-for example, contributing to a higher order ... On the other hand, frogs and chickens have domains in their chaperones that are not at all shared with that of yeast. Hence, ... However, even though the CENPA histone variant is in fact conserved, there is a surprisingly large amount of diversity in the ...
One such class of cellular proteins is the nucleoplasmins, which serve as molecular chaperone proteins for histone assembly ... Examples include the non-heme dioxygenase enzymes and JmjC-family histone demethylases. Comparative studies of proteins ... Klose, Robert J.; Zhang, Yi (7 March 2007). "Regulation of histone methylation by demethylimination and demethylation". Nature ... "Structural Insights into Histone Demethylation by JMJD2 Family Members". Cell. 125 (4): 691-702. doi:10.1016/j.cell.2006.04.024 ...
Deletion of the highly acidic carboxy-terminus of Spt16 (a common feature of known histone chaperones) does not prevent Spt16 ... The two subunits together, but neither alone, can stimulate formation of nucleosomes from free histones and DNA (histone ... and purified human FACT binds specifically to mononucleosomes and the histone H2A/H2B dimer, but not to the H3/H4 tetramer (see ... chaperone activity). These two subunits are highly conserved across all eukaryotes, and in addition to transcription, have been ...
Histones are important in the process of gene expression, and their positioning as determined by chaperone proteins is ... The chaperones also can change the conformation of the nucleosome as a whole. Modifications to histones, including acetylation ... She also proposed that histone-DNA bonds are weaker at points where less of the histone contacts the DNA, which was confirmed ... Luger has done significant studies of histones, researching the connection between their chaperone proteins and acetylation, as ...
Though chloroplast DNA is not associated with true histones,[15] in red algae, a histone-like chloroplast protein (HC) coded by ... 4.2 Phosphorylation, chaperones, and transport. *4.3 The translocon on the outer chloroplast membrane (TOC) *4.3.1 Toc34 and 33 ... Phosphorylation, chaperones, and transportEdit. After a chloroplast polypeptide is synthesized on a ribosome in the cytosol, ...
... the ASF1 like histone chaperone family of proteins includes the yeast and human ASF1 proteins. These proteins have histone ... "A human homologue of yeast anti-silencing factor has histone chaperone activity". Genes Cells. 5 (3): 221-33. doi:10.1046/j. ... "Structure and function of the conserved core of histone deposition protein Asf1". Curr. Biol. 13 (24): 2148-58. doi:10.1016/j. ... chaperone activity. ASF1 participates in both the replication-dependent and replication-independent pathways. The three- ...
... firmly placing AM-PARP-1 in the league of bona fide histone chaperones (27). Histone chaperones are defined as nuclear proteins ... 2010) The histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone DNA interactions. Mol Cell ... 3E, lanes 11-13). This demonstrates that PARylation of PARP-1, but not of histones, is required for its histone chaperone and ... The ability of a histone chaperone to prevent noncanonical interactions of histones with DNA and nucleosomes might be important ...
Initially, function of histone chaperones was thought to be only ... Histones, the structural unit of chromatin, must be assembled/ ... Initially, function of histone chaperones was thought to be only "histone carriers/vehicles", but now with accumulating ... Park, Y.J. and Luger, K. (2008) Histone Chaperones in Nucleosome Eviction and Histone Exchange. Current Opinion in Structural ... The Histone Chaperone Anti-Silencing Function 1 Stimulates the Acetylation of Newly Synthesized Histone H3 in S-Phase. Journal ...
... histones do contain acidic patches that have previously been implicated in histone-histone interactions (1). Therefore, histone ... Indeed, the histone chaperone Asf1 uses distinct histone-binding surfaces for H3 and H4 (30). Consistent with this idea, the ... Chaperone:histone interactions are influenced by histone type and oligomeric status (3, 4). However, much less is known about ... 2010) The histone shuffle: Histone chaperones in an energetic dance. Trends Biochem Sci 35:476-489. ...
... Xavier Gaume,1 Karine Monier,1 Françoise Argoul,1,2 ... Nucleolin possesses, in vitro, chromatin co-remodeler and histone chaperone activities which could explain numerous functions ... Thus, in live cells, nucleolin could play a role in chromatin accessibility by its histone chaperone and co-remodeling ... Changes in histone dynamics occurring in nucleolin silenced cells were measured by FRAP experiments on eGFP-tagged histones ( ...
Shortly after that, the CIA-histone-H3-H4 complex was isolated from Drosophila as a histone chaperone CAF-1 stimulator2. Human ... was identified as a histone chaperone that interacts with the bromodomain-an acetylated-histone-recognizing domain-of CCG1, in ... The mechanism of nucleosome assembly and disassembly has been elusive but now the crystal structure of a histone chaperone in ... CIA/ASF1 was shown as a major storage chaperone for soluble histones in proliferating human cells6,16. Despite all these ...
Developmental roles of histone H3 variants and their chaperones.. Filipescu D1, Szenker E, Almouzni G. ... promoted by dedicated histone chaperones. Moreover, their individual modifications and binding partners provide distinct ... Histone H3 variants contribute to chromatin dynamics through the timing and sites of their incorporation, ... Future challenges will be to gain a comprehensive picture of H3 variants and their chaperones during development and ...
Rtt109 associates with the NAP1 family histone chaperone Vps75 and stimulates histone acetylation. Here we explore the ... Rtt109 is a histone acetyltransferase (HAT) involved in promoting genomic stability, DNA repair, and transcriptional regulation ... mechanism of histone acetylation and report a detail … ... Rtt109 associates with the NAP1 family histone chaperone Vps75 ... Kinetic mechanism of the Rtt109-Vps75 histone acetyltransferase-chaperone complex Biochemistry. 2010 Aug 3;49(30):6375-85. doi ...
The histone chaperone chromatin assembly factor 1 (CAF-1) mediates histone H3-H4 assembly during DNA replication and nucleotide ... This is mediated in part by the histone chaperone chromatin assembly factor 1 (CAF-1), which deposits histones H3 and H4 onto ... Adkins, M. W., S. R. Howar and J. K. Tyler, 2004 Chromatin disassembly mediated by the histone chaperone Asf1 is essential for ... Adkins, M. W., and J. K. Tyler, 2004 The histone chaperone Asf1p mediates global chromatin disassembly in vivo. J. Biol. Chem. ...
66: 2.35 Å structure of the Sp16M chaperone domain (orange/red) in complex with histones H2A-H2B (light green-blue). The ... We found that electrostatic interactions contribute to the stability of the histone-chaperone complex. First, the basic N- ... Furthermore, we found that Spt16M also recognises histones H3-H4. Similar to the structurally related chaperone Rtt106, Spt16M ... How the chaperone FACT recognises histones H2A-H2B and mediates nucleosome reorganisation. ...
Here we report the structure of a histone/histone chaperone interaction. We have solved the 2.2 A crystal structure of the ... The histone H3/H4 chaperone Asf1 (anti-silencing function 1) is required for the establishment and maintenance of proper ... Genetic analysis of Asf1 residues important for histone binding. Asf1 histone binding mutants cause silencing defects in vivo. ... Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and ...
Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF and ... In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their ... Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of ... RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. ...
... scientists knew that the histone chaperone Rtt106 helped in the deposition of histones - specifically, a complex of histones H3 ... Associated with the histones is another group of proteins called histone chaperones, which promote the proper assembly or ... This is the first time anyone has described this mode of specific association between a histone chaperone and a modified ... Home Medical Breakthroughs Mayo Researchers Provide Atomic View of a Histone Chaperone ...
Results We established a strain of S. cerevisiae lacking the histone chaperone ASF1/CIA1. This disruptant, asf1/cia1, arrested ... The factor hCIA interacts with hCCG1 and functions as a histone chaperone in mammalian cells; its homologue in yeast is Asf1p/ ... Cell death with predominant apoptotic features in Saccharomyces cerevisiae mediated by deletion of the histone chaperone ASF1/ ... elegans homologs of the histone chaperone Asf1 in germline DNA replication, Developmental Biology, 2009, 329, 1, 64. CrossRef ...
... is a histone chaperone that can destabilize or assemble nucleosomes. Acetylation of histone H3-K56 weakens a histone-DNA ... Establishment and Maintenance of Chromatin Architecture Are Promoted Independently of Transcription by the Histone Chaperone ... Establishment and Maintenance of Chromatin Architecture Are Promoted Independently of Transcription by the Histone Chaperone ... Establishment and Maintenance of Chromatin Architecture Are Promoted Independently of Transcription by the Histone Chaperone ...
DNA damage-specific histone chaperone Aprataxin PNK-like factor (APLF) regulates mesenchymal-to-epithelial transition (MET) ... As a histone chaperone, APLF specifically bind to histones H3/H4 tetramer and could recruit variants of histone H2A at the ... Histone chaperones in nature could interact with histone modifying enzymes and thereby could modulate different histone ... DNA repair factor APLF is a histone chaperone. Mol Cell. 2011;41:46-55.CrossRefPubMedPubMedCentralGoogle Scholar ...
Histone octamer-histone chaperone complex was formed by incubating 600 ng of core histone octamer (core histones HeLa; ... OsNAPL6 Is an H3/H4 Histone Chaperone. Most of the histone chaperones are known to be specific to either the H3/H4 or H2A/H2B ... Subcellular localization of a histone chaperone defines its exact function. For example, a nuclear-localized histone chaperone ... histone chaperone of the NAP superfamily: OsNAPL6. We show that OsNAPL6 is a nuclear-localized H3/H4 histone chaperone capable ...
Chaperone co-inducer BGP-15 inhibits histone deacetylases and enhances the heat shock response through increased chromatin ... HATs histone acetyltransferases, HDACs histone deacetylases, HDACi HDAC inhibitors, HSPs heat shock proteins ... Cell Stress Chaperones 17:517-521. doi: 10.1007/s12192-012-0327-5 CrossRefPubMedPubMedCentralGoogle Scholar ... Cell Stress Chaperones 20:185-201. doi: 10.1007/s12192-014-0536-1 CrossRefPubMedPubMedCentralGoogle Scholar ...
2015 Dissecting the Molecular Roles of Histone Chaperones in Histone Acetylation by Type B Histone Acetyltransferases (HAT-B). ... 2012 Histone chaperones link histone nuclear import and chromatin assembly. Biochim. Biophys. Acta 1819: 277-289. doi:10.1016/j ... 2007 Histone chaperones: an escort network regulating histone traffic. Nat. Struct. Mol. Biol. 14: 997-1007. doi:10.1038/ ... 2016 The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats ...
About the Cover Chaperone HJURP drives the proper loading of protein CENP-A to the centromere of a chromosome. The effect of ... Promiscuous histone mis-assembly is actively prevented by chaperones. Zhao, Haiqing+; Winogradoff, David+; Bui, Minh; Dalal, ... Our data show that the H4 histone is significantly more rigid compared with the H3 histone and its variant CENP-A, hence, ... Chaperone HJURP drives the proper loading of protein CENP-A to the centromere of a chromosome. The effect of HJURP on CENP-As ...
Elucidating the molecular mechanisms conferred by the histone chaperone FACT. PhD thesis, Universität zu Köln. ... The conserved and essential histone chaperone FACT (Facilitates Chromatin Transcription) reorganises nucleosomes during DNA ...
This observation lead us to investigate the status of histones and histone chaperone NPM1 acetylation in oral cancer patient ... Accueil du site , Animations Scientifiques , Séminaires 2009 , Tapas K. Kundu - Acetylation of Histones and Histone Chaperones ... Acetylation of Histones and Histone Chaperones in Cancer Manifestation : Implications in Therapeutics ... Tapas K. Kundu - Acetylation of Histones and Histone Chaperones in Cancer Manifestation : Implications in Therapeutics. ...
2014). Histone chaperones: assisting histone traffic and nucleosome dynamics. Annu. Rev. Biochem. 83, 487-517. doi:10.1146/ ... HIRA is the histone chaperone responsible for replication-independent incorporation of histone variant H3.3 within gene bodies ... 2013). Histone chaperones in nucleosome assembly and human disease. Nat. Struct. Mol. Biol. 20, 14-22. doi:10.1038/nsmb.2461. ... 2015). Histone chaperone HIRA in regulation of transcription factor RUNX1. J. Biol. Chem. 290, 13053-13063. doi:10.1074/jbc. ...
Recombinant Protein and Histone H2A.Z-specific chaperone Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and ... Shop Histone H2A.Z-specific chaperone ELISA Kit, ... Histone H2A.Z-specific chaperone chz-1. Histone H2A.Z-specific ... Histone H2A.Z-specific chaperone chz1. Histone H2A.Z-specific chaperone chz1 ELISA Kit. Histone H2A.Z-specific chaperone chz1 ... Histone H2A.Z-specific chaperone chz-1 Recombinant. Histone H2A.Z-specific chaperone chz-1 Antibody. Forms a chaperone-bound ...
For the largest histone chaperone family, NAP, phylogenetic reconstruction suggested the presence of two distinct groups in ... Phylogenetic analyses of histone chaperones from diverse organisms including representative species from each of the major ... In contrast to their animal and yeast counterparts, not much is known about plant histone chaperones. To gain insights into ... Taken together, our findings shed light onto the possible evolutionary trajectory of plant histone chaperones and present novel ...
  • When histone binding was compromised, Rtt106 localized properly to chromatin but failed to deliver H3K56ac, leading to replication and silencing defects. (pnas.org)
  • Our studies described the structural origins of Rtt106 function, identified a conserved histone-binding surface, and defined a critical role for Rtt106:H3K56ac-binding specificity in silencing and replication-coupled nucleosome turnover. (pnas.org)
  • She did her postdoctoral training from 2005 to 2007 with Dr. Almouzni at Institut Curie, Paris, focusing on histone dynamics during DNA replication. (ku.dk)
  • Here, we biochemically demonstrated that the DNA/nucleosome and histone chaperone binding activities of H1.X are significantly lower than those of other linker histones. (asm.org)
  • This explains why H1.X moves more rapidly than other linker histones in vivo . (asm.org)
  • We also found that linker histones accumulate in the nucleoli when the nucleosome binding activities of the GDs are weak. (asm.org)
  • Histones, including linker histones, are highly basic proteins that randomly bind to DNA. (asm.org)
  • Linker histones are comprised of three regions: the N-terminal domain (NTD), central globular domain (GD), and C-terminal domain (CTD). (asm.org)
  • The CTD of linker histones are generally basic and rich in lysines, alanines, and prolines. (asm.org)
  • Fluorescent recovery after photobleaching (FRAP) assays using various combinations of mutant linker histones have demonstrated that both the GD and CTD cooperatively contribute to the stable binding of linker histones on chromatin ( 11 ). (asm.org)
  • Linker histones bind to the linker DNA regions at the entry and exit sites of the nucleosome resulting in a structure that protects the DNA from digestion by micrococcal nuclease by an additional 20-22 bp termed as chromatosome [ 8 ]. (portlandpress.com)
  • I am uncovering novel biological roles for an evolutionarily conserved histone chaperone. (mit.edu)
  • Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release. (yu.edu)
  • Ravi and Chan (2010 ) discovered that haploids could be obtained in Arabidopsis through the manipulation of the centromere-specific histone 3 variant, CENH3. (frontiersin.org)