Acetyltransferases: Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.Histone Acetyltransferases: Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.Acetylation: Formation of an acetyl derivative. (Stedman, 25th ed)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.N-Terminal Acetyltransferases: Enzymes that catalyze the transfer of an acetyl group, usually from ACETYL COENZYME A, to the N-terminus of a peptide chain.Carnitine O-Acetyltransferase: An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.CREB-Binding Protein: A member of the p300-CBP transcription factor family that was initially identified as a binding partner for CAMP RESPONSE ELEMENT-BINDING PROTEIN. Mutations in CREB-binding protein are associated with RUBINSTEIN-TAYBI SYNDROME.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.E1A-Associated p300 Protein: A member of the p300-CBP transcription factors that was originally identified as a binding partner for ADENOVIRUS E1A PROTEINS.N-Terminal Acetyltransferase E: An N-terminal acetyltransferase subtype that consists of the Naa50p catalytic subunit, and the Naa10p and Naa15p auxiliary subunits. It has specificity for the N-terminal METHIONINE of peptides where the next amino acid in the chain is hydrophobic.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.Acetyl Coenzyme A: Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.Lysine: An essential amino acid. It is often added to animal feed.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.N-Terminal Acetyltransferase A: An N-terminal acetyltransferase subtype that consists of the Naa10p catalytic subunit and the Naa15p auxiliary subunit. The structure of this enzyme is conserved between lower and higher eukaryotes. It has specificity for N-terminal SERINE; ALANINE; THREONINE; GLYCINE; VALINE; and CYSTINE residues and acts on nascent peptide chains after the removal of the initiator METHIONINE by METHIONYL AMINOPEPTIDASES.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.Anacardic Acids: A group of 6-alkyl SALICYLIC ACIDS that are found in ANACARDIUM and known for causing CONTACT DERMATITIS.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.Trans-Activators: Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.Arylamine N-Acetyltransferase: An enzyme that catalyzes the transfer of acetyl groups from ACETYL-COA to arylamines. It can also catalyze acetyl transfer between arylamines without COENZYME A and has a wide specificity for aromatic amines, including SEROTONIN. However, arylamine N-acetyltransferase should not be confused with the enzyme ARYLALKYLAMINE N-ACETYLTRANSFERASE which is also referred to as SEROTONIN ACETYLTRANSFERASE.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.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.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.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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.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.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.Transcriptional Activation: Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.Amino-Acid N-Acetyltransferase: A mitochondrial matrix enzyme that catalyzes the synthesis of L-GLUTAMATE to N-acetyl-L-glutamate in the presence of ACETYL-COA.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.Hydroxamic Acids: A class of weak acids with the general formula R-CONHOH.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.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.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.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.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.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.Alkanes: The generic name for the group of aliphatic hydrocarbons Cn-H2n+2. They are denoted by the suffix -ane. (Grant & Hackh's Chemical Dictionary, 5th ed)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.Histone Chaperones: Proteins involved in the assembly and disassembly of HISTONES into NUCLEOSOMES.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.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.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.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.Adenovirus E1A Proteins: Proteins transcribed from the E1A genome region of ADENOVIRUSES which are involved in positive regulation of transcription of the early genes of host infection.Nuclear Receptor Coactivator 2: A transcription factor that partners with ligand bound GLUCOCORTICOID RECEPTORS and ESTROGEN RECEPTORS to stimulate GENETIC TRANSCRIPTION. It plays an important role in FERTILITY as well as in METABOLISM of LIPIDS.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)Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.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.Cell Line: Established cell cultures that have the potential to propagate indefinitely.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.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.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Gene Expression Regulation, Fungal: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in fungi.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Precipitin Tests: Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Biocatalysis: The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.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.Fungal Proteins: Proteins found in any species of fungus.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.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-Arginine N-Methyltransferases: Enzymes that catalyze the methylation of arginine residues of proteins to yield N-mono- and N,N-dimethylarginine. This enzyme is found in many organs, primarily brain and spleen.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Gene Products, tat: Trans-acting transcription factors produced by retroviruses such as HIV. They are nuclear proteins whose expression is required for viral replication. The tat protein stimulates LONG TERMINAL REPEAT-driven RNA synthesis for both viral regulatory and viral structural proteins. tat stands for trans-activation of transcription.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Aminoglycosides: Glycosylated compounds in which there is an amino substituent on the glycoside. Some of them are clinically important ANTIBIOTICS.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)Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.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.Gene Silencing: Interruption or suppression of the expression of a gene at transcriptional or translational levels.tat Gene Products, Human Immunodeficiency Virus: Proteins encoded by the TAT GENES of the HUMAN IMMUNODEFICIENCY VIRUS.Blotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Kinetics: The rate dynamics in chemical or physical systems.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.Luciferases: Enzymes that oxidize certain LUMINESCENT AGENTS to emit light (PHYSICAL LUMINESCENCE). The luciferases from different organisms have evolved differently so have different structures and substrates.Reverse Transcriptase Polymerase Chain Reaction: A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Cell Line, Tumor: A cell line derived from cultured tumor cells.Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.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.Genes, Reporter: Genes whose expression is easily detectable and therefore used to study promoter activity at many positions in a target genome. In recombinant DNA technology, these genes may be attached to a promoter region of interest.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.3T3 Cells: Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION.COS Cells: CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)Multigene Family: A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Immunoprecipitation: The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.RNA Interference: A gene silencing phenomenon whereby specific dsRNAs (RNA, DOUBLE-STRANDED) trigger the degradation of homologous mRNA (RNA, MESSENGER). The specific dsRNAs are processed into SMALL INTERFERING RNA (siRNA) which serves as a guide for cleavage of the homologous mRNA in the RNA-INDUCED SILENCING COMPLEX. DNA METHYLATION may also be triggered during this process.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.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Bacterial Proteins: Proteins found in any species of bacterium.Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.Sequence Deletion: Deletion of sequences of nucleic acids from the genetic material of an individual.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Gene Expression Regulation, Developmental: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action during the developmental stages of an organism.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Protein Subunits: Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.Macromolecular Substances: Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.Genes, Fungal: The functional hereditary units of FUNGI.
(1/3280) Prodigious substrate specificity of AAC(6')-APH(2"), an aminoglycoside antibiotic resistance determinant in enterococci and staphylococci.

BACKGROUND: High-level gentamicin resistance in enterococci and staphylococci is conferred by AAC(6')-APH(2"), an enzyme with 6'-N-acetyltransferase and 2"-O-phosphotransferase activities. The presence of this enzyme in pathogenic gram-positive bacteria prevents the successful use of gentamicin C and most other aminoglycosides as therapeutic agents. RESULTS: In an effort to understand the mechanism of aminoglycoside modification, we expressed AAC(6')-APH(2") in Bacillus subtilis. The purified enzyme is monomeric with a molecular mass of 57 kDa and displays both the expected aminoglycoside N-acetyltransferase and O-phosphotransferase activities. Structure-function analysis with various aminoglycosides substrates reveals an enzyme with broad specificity in both enzymatic activities, accounting for AAC(6')-APH(2")'s dramatic negative impact on clinical aminoglycoside therapy. Both lividomycin A and paromomycin, aminoglycosides lacking a 6'-amino group, were acetylated by AAC(6')-APH(2"). The infrared spectrum of the product of paromomycin acetylation yielded a signal consistent with O-acetylation. Mass spectral and nuclear magnetic resonance analysis of the products of neomycin phosphorylation indicated that phosphoryl transfer occurred primarily at the 3'-OH of the 6-aminohexose ring A, and that some diphosphorylated material was also present with phosphates at the 3'-OH and the 3"'-OH of ring D, both unprecedented observations for this enzyme. Furthermore, the phosphorylation site of lividomycin A was determined to be the 5"-OH of the pentose ring C. CONCLUSIONS: The bifunctional AAC(6')-APH(2") has the capacity to inactivate virtually all clinically important aminoglycosides through N- and O-acetylation and phosphorylation of hydroxyl groups. The extremely broad substrate specificity of this enzyme will impact on future development of aminoglycosides and presents a significant challenge for antibiotic design.  (+info)

(2/3280) The amino-terminal C/H1 domain of CREB binding protein mediates zta transcriptional activation of latent Epstein-Barr virus.

Latent Epstein-Barr virus (EBV) is maintained as a nucleosome-covered episome that can be transcriptionally activated by overexpression of the viral immediate-early protein, Zta. We show here that reactivation of latent EBV by Zta can be significantly enhanced by coexpression of the cellular coactivators CREB binding protein (CBP) and p300. A stable complex containing both Zta and CBP could be isolated from lytically stimulated, but not latently infected RAJI nuclear extracts. Zta-mediated viral reactivation and transcriptional activation were both significantly inhibited by coexpression of the E1A 12S protein but not by an N-terminal deletion mutation of E1A (E1ADelta2-36), which fails to bind CBP. Zta bound directly to two related cysteine- and histidine-rich domains of CBP, referred to as C/H1 and C/H3. These domains both interacted specifically with the transcriptional activation domain of Zta in an electrophoretic mobility shift assay. Interestingly, we found that the C/H3 domain was a potent dominant negative inhibitor of Zta transcriptional activation function. In contrast, an amino-terminal fragment containing the C/H1 domain was sufficient for coactivation of Zta transcription and viral reactivation function. Thus, CBP can stimulate the transcription of latent EBV in a histone acetyltransferase-independent manner mediated by the CBP amino-terminal C/H1-containing domain. We propose that CBP may regulate aspects of EBV latency and reactivation by integrating cellular signals mediated by competitive interactions between C/H1, C/H3, and the Zta activation domain.  (+info)

(3/3280) The histone acetylase PCAF is a phorbol-ester-inducible coactivator of the IRF family that confers enhanced interferon responsiveness.

Transcription factors of the interferon regulatory factor (IRF) family bind to the type I interferon (IFN)-responsive element (ISRE) and activate transcription from IFN-inducible genes. To identify cofactors that associate with IRF proteins, DNA affinity binding assays were performed with nuclear extracts prepared from tissue culture cells. The results demonstrated that the endogenous IRFs bound to the ISRE are complexed with the histone acetylases, PCAF, GCN5, and p300/CREB binding protein and that histone acetylase activities are accumulated on the IRF-ISRE complexes. By testing recombinant proteins, we show that PCAF directly binds to some but not all members of the IRF family through distinct domains of the two proteins. This interaction was functionally significant, since transfection of PCAF strongly enhanced IRF-1- and IRF-2-dependent promoter activities. Further studies showed that expression of PCAF and other histone acetylases was markedly induced in U937 cells upon phorbol ester treatment, which led to increased recruitment of PCAF to the IRF-ISRE complexes. Coinciding with the induction of histone acetylases, phorbol ester markedly enhanced IFN-alpha-stimulated gene expression in U937 cells. Supporting the role for PCAF in conferring IFN responsiveness, transfection of PCAF into U937 cells led to a large increase in IFN-alpha-inducible promoter activity. These results demonstrate that PCAF is a phorbol ester-inducible coactivator of the IRF proteins which contributes to the establishment of type I IFN responsiveness.  (+info)

(4/3280) A novel H2A/H4 nucleosomal histone acetyltransferase in Tetrahymena thermophila.

Recently, we reported the identification of a 55-kDa polypeptide (p55) from Tetrahymena macronuclei as a catalytic subunit of a transcription-associated histone acetyltransferase (HAT A). Extensive homology between p55 and Gcn5p, a component of the SAGA and ADA transcriptional coactivator complexes in budding yeast, suggests an immediate link between the regulation of chromatin structure and transcriptional output. Here we report the characterization of a second transcription-associated HAT activity from Tetrahymena macronuclei. This novel activity is distinct from complexes containing p55 and putative ciliate SAGA and ADA components and shares several characteristics with NuA4 (for nucleosomal H2A/H4), a 1.8-MDa, Gcn5p-independent HAT complex recently described in yeast. A key feature of both the NuA4 and Tetrahymena activities is their acetylation site specificity for lysines 5, 8, 12, and 16 of H4 and lysines 5 and 9 of H2A in nucleosomal substrates, patterns that are distinct from those of known Gcn5p family members. Moreover, like NuA4, the Tetrahymena activity is capable of activating transcription from nucleosomal templates in vitro in an acetyl coenzyme A-dependent fashion. Unlike NuA4, however, sucrose gradient analyses of the ciliate enzyme, following sequential denaturation and renaturation, estimate the molecular size of the catalytically active subunit to be approximately 80 kDa, consistent with the notion that a single polypeptide or a stable subcomplex is sufficient for this H2A/H4 nucleosomal HAT activity. Together, these data document the importance of this novel HAT activity for transcriptional activation from chromatin templates and suggest that a second catalytic HAT subunit, in addition to p55/Gcn5p, is conserved between yeast and Tetrahymena.  (+info)

(5/3280) In vivo and in vitro processing of the Bacillus subtilis transcript coding for glutamyl-tRNA synthetase, serine acetyltransferase, and cysteinyl-tRNA synthetase.

In Bacillus subtilis, the adjacent genes gltX, cysE, and cysS encoding respectively glutamyl-tRNA synthetase, serine acetyl-transferase, and cysteinyl-tRNA synthetase, are transcribed as an operon but a gltX probe reveals only the presence of a monocistronic gltX mRNA (Gagnon et al., 1994, J Biol Chem 269:7473-7482). The transcript of the gltX-cysE intergenic region contains putative alternative secondary structures forming a p-independent terminator or an antiterminator, and a conserved sequence (T-box) found in the leader of most aminoacyl-tRNA synthetase and many amino acid biosynthesis genes in B. subtilis and in other Gram-positive eubacteria. The transcription of these genes is initiated 45 nt upstream from the first codon of gltX and is under the control of a sigmaA-type promoter. Analysis of the in vivo transcript of this operon revealed a cleavage site immediately downstream from the p-independent terminator structure. In vitro transcription analysis, using RNA polymerases from Escherichia coli, B. subtilis, and that encoded by the T7 phage, in the presence of various RNase inhibitors, shows the same cleavage. This processing generates mRNAs whose 5'-end half-lives differ by a factor of 2 in rich medium, and leaves putative secondary structures at the 3' end of the gltX transcript and at the 5' end of the cysE/S mRNA, which may be involved in the stabilization of these mRNAs. By its mechanism and its position, this cleavage differs from that of the other known transcripts encoding aminoacyl-tRNA synthetases in B. subtilis.  (+info)

(6/3280) Overexpression of spermidine/spermine N1-acetyltransferase under the control of mouse metallothionein I promoter in transgenic mice: evidence for a striking post-transcriptional regulation of transgene expression by a polyamine analogue.

We recently generated a transgenic mouse line overexpressing spermidine/spermine N1-acetyltransferase (SSAT) gene under its own promoter. The tissue polyamine pools of these animals were profoundly affected and the mice were hairless from early age. We have now generated another transgenic-mouse line overexpressing the SSAT gene under the control of a heavy-metal-inducible mouse metallothionein I (MT) promoter. Even in the absence of heavy metals, changes in the tissue polyamine pools indicated that a marked activation of polyamine catabolism had occurred in the transgenic animals. As with the SSAT transgenic mice generated previously, the mice of the new line (MT-SSAT) suffered permanent hair loss, but this occurred considerably later than in the previous SSAT transgenic animals. Liver was the most affected tissue in the MT-SSAT transgenic animals, revealed by putrescine overaccumulation, significant decrease in spermidine concentration and >90% reduction in the spermine pool. Even though hepatic SSAT mRNA accumulated to massive levels in non-induced transgenic animals, SSAT activity was only moderately elevated. Administration of ZnSO4 further elevated the level of hepatic SSAT message and induced enzyme activity, but not more than 2- to 3-fold. Treatment of the transgenic animals with the polyamine analogue N1,N11-diethylnorspermine (DENSPM) resulted in an immense induction, more than 40000-fold, of enzyme activity in the liver of transgenic animals, and minor changes in the SSAT mRNA level. Liver spermidine and spermine pools were virtually depleted within 1-2 days in response to the treatment with the analogue. The treatment also resulted in a marked mortality (up to 60%) among the transgenic animals which showed ultrastructural changes in the liver, most notably mitochondrial swelling, one of the earliest signs of cell injury. These results indicated that, even without its own promoter, SSAT is powerfully induced by the polyamine analogue through a mechanism that appears to involve a direct translational and/or heterogenous nuclear RNA processing control. It is likewise significant that overexpression of SSAT renders the animals extremely sensitive to polyamine analogues.  (+info)

(7/3280) Virus infection leads to localized hyperacetylation of histones H3 and H4 at the IFN-beta promoter.

Transcriptional activation of the human interferon-beta (IFN-beta) gene by virus infection requires the assembly of a higher order nucleoprotein complex, the enhanceosome, which consists of the transcriptional activators NF-kappa B (p50/p65), ATF-2/c-jun, IRF-3 and IRF-7, architectural protein HMGI(Y), and the coactivators p300 and CBP. In this report, we show that virus infection of cells results in a dramatic hyperacetylation of histones H3 and H4 that is localized to the IFN-beta promoter. Furthermore, expressing a truncated version of IRF-3, which lacks a p300/CBP interaction domain, suppresses both histone hyperacetylation and activation of the IFN-beta gene. Thus, coactivator-mediated localized hyperacetylation of histones may play a crucial role in inducible gene expression.  (+info)

(8/3280) A viral mechanism for inhibition of p300 and PCAF acetyltransferase activity.

Nucleosomal histone modification is believed to be a critical step in the activation of RNA polymerase II-dependent transcription. p300/CBP and PCAF histone acetyltransferases (HATs) are coactivators for several transcription factors, including nuclear hormone receptors, p53, and Stat1alpha, and participate in transcription by forming an activation complex and by promoting histone acetylation. The adenoviral E1A oncoprotein represses transcriptional signaling by binding to p300/CBP and displacing PCAF and p/CIP proteins from the complex. Here, we show that E1A directly represses the HAT activity of both p300/CBP and PCAF in vitro and p300-dependent transcription in vivo. Additionally, E1A inhibits nucleosomal histone modifications by the PCAF complex and blocks p53 acetylation. These results demonstrate the modulation of HAT activity as a novel mechanism of transcriptional regulation.  (+info)

*  Histone acetyltransferase
RNA polymerase control by chromatin structure Acetyltransferase Lee KK, Workman JL (April 2007). "Histone acetyltransferase ... Histone acetyltransferases serve many biological roles inside the cell. Chromatin is a combination of proteins and DNA found in ... If histone acetyltransferases are inhibited, then damaged DNA may not be repaired, eventually leading to cell death. ... Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring ...
*  N-acetyltransferase 1
... (arylamine N-acetyltransferase) is a protein that in humans is encoded by the NAT1 gene. This gene is one ... N-acetyltransferase 1 (arylamine N-acetyltransferase)". Retrieved 2012-01-27. Gubin AN, Njoroge JM, Bouffard GG, Miller JL ( ... Yu MW, Pai CI, Yang SY, Hsiao TJ, Chang HC, Lin SM, Liaw YF, Chen PJ, Chen CJ (November 2000). "Role of N-acetyltransferase ... Brockton N, Little J, Sharp L, Cotton SC (May 2000). "N-acetyltransferase polymorphisms and colorectal cancer: a HuGE review". ...
*  Acetyltransferase
... acetyltransferase Chloramphenicol acetyltransferase Serotonin N-acetyltransferase NatA Acetyltransferase NatB acetyltransferase ... Examples include: Histone acetyltransferases including CBP histone acetyltransferase Choline ... Acetyltransferase (or transacetylase) is a type of transferase enzyme that transfers an acetyl group. ... Acyltransferase Acetylation Acetyltransferases at the US National Library of Medicine Medical Subject Headings (MeSH). ...
*  N-acetyltransferase
... is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to arylamines. They have wide ... 50% of the British population are deficient in hepatic N-acetyltransferase. This is known as a negative acetylator status. ... "N-acetyltransferase". Pharmacology & Therapeutics. 42 (2): 157-234. doi:10.1016/0163-7258(89)90036-3. PMID 2664821. Ma Y, ... isoniazid procainamide hydralazine dapsone sulfasalazine The following is a list of human genes that encode N-acetyltransferase ...
*  Chloramphenicol acetyltransferase
... (or CAT) is a bacterial enzyme (EC 2.3.1.28) that detoxifies the antibiotic chloramphenicol ... Leslie AG (1990). "Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75 A resolution". J. Mol. Biol ... Gorman, CM; Moffat LF; Howard BH (1982). "Recombinant genomes which express chloramphenicol acetyltransferase in mammalian ... "Primary structure of a chloramphenicol acetyltransferase specified by R plasmids". Nature. 282 (5741): 870-2. doi:10.1038/ ...
*  NatA acetyltransferase
... (Nα acetyltransferase), is an enzyme that serves to catalyze the addition of acetyl groups to various ... NatA Acetyltransferase is not a single protein but a complex of three subunits. In Saccharomyces cerevisiae NatA ... "The NatA Acetyltransferase Couples Sup35 Prion Complexes to the [PSI ] Phenotype - Pezza et al. 20 (3): 1068- ." Molecular ... To be specific, NatA is the main N{alpha}-terminal acetyltransferase in the yeast cytosol, responsible for the acetylation of ...
*  Phosphinothricin acetyltransferase
... (EC 2.3.1.183, PAT, PPT acetyltransferase, Pt-N-acetyltransferase, ac-Pt) is an enzyme with ... Phosphinothricin acetyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... Botterman, J.; Gosselé, V.; Thoen, C.; Lauwereys, M. (1991). "Characterization of phosphinothricin acetyltransferase and C- ... systematic name acetyl-CoA:phosphinothricin N-acetyltransferase. This enzyme catalyses the following chemical reaction acetyl- ...
*  Choline acetyltransferase
In humans, the choline acetyltransferase enzyme is encoded by the CHAT gene. Choline acetyltransferase was first described by ... Choline Acetyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Choline acetyltransferase (commonly abbreviated as ChAT, but sometimes CAT) is a transferase enzyme responsible for the ... Strauss WL, Kemper RR, Jayakar P, Kong CF, Hersh LB, Hilt DC, Rabin M (1991). "Human choline acetyltransferase gene maps to ...
*  Phosphate acetyltransferase
In enzymology, a phosphate acetyltransferase (EC 2.3.1.8) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... The systematic name of this enzyme class is acetyl-CoA:phosphate acetyltransferase. Other names in common use include ...
*  PAF acetyltransferase
... may refer to: 1-alkylglycerophosphocholine O-acetyltransferase Platelet-activating factor ...
*  Diaminobutyrate acetyltransferase
... diaminobutyric acid acetyltransferase, DABA acetyltransferase, 2,4-diaminobutanoate acetyltransferase, DAB acetyltransferase, ... Other names in common use include L-2,4-diaminobutyrate acetyltransferase, L-2,4-diaminobutanoate acetyltransferase, EctA, ... In enzymology, a diaminobutyrate acetyltransferase (EC 2.3.1.178) is an enzyme that catalyzes the chemical reaction acetyl-CoA ... The systematic name of this enzyme class is acetyl-CoA:L-2,4-diaminobutanoate N4-acetyltransferase. ...
*  Sulfoacetaldehyde acetyltransferase
In enzymology, a sulfoacetaldehyde acetyltransferase (EC 2.3.3.15) is an enzyme that catalyzes the chemical reaction acetyl ... The systematic name of this enzyme class is acetyl-phosphate:sulfite S-acetyltransferase (acyl-phosphate hydrolysing, 2- ... Ruff J, Denger K, Cook AM (2003). "Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification from Alcaligenes ...
*  NatB acetyltransferase
... is an enzyme in the Saccharomyces cerevisiae that functions to catalyze the dehydration synthesis of the ...
*  N-acetyltransferase 2
... (arylamine N-acetyltransferase), also known as NAT2, is an enzyme which in humans is encoded by the NAT2 ... "Entrez Gene: NAT2 N-acetyltransferase 2 (arylamine N-acetyltransferase)". "NAT2PRED: a computational predictor of the human N- ... Sanderson S, Salanti G, Higgins J (2007). "Joint effects of the N-acetyltransferase 1 and 2 (NAT1 and NAT2) genes and smoking ... Ochs-Balcom HM, Wiesner G, Elston RC (2007). "A meta-analysis of the association of N-acetyltransferase 2 gene (NAT2) variants ...
*  Carnitine O-acetyltransferase
... also called carnitine acetyltransferase (CRAT, or CAT) (EC 2.3.1.7) is an enzyme that encoded by ... In general, carnitine acetyltransferases have molecular weights of about 70 kDa, and contain approximately 600 residues1. CRAT ... The systematic name of this enzyme class is acetyl-CoA:carnitine O-acetyltransferase. Other names in common use include acetyl- ... Hsiao YS, Jogl G, Tong L (Sep 2006). "Crystal structures of murine carnitine acetyltransferase in ternary complexes with its ...
*  Aralkylamine N-acetyltransferase
The N-acetyltransferase reaction has been suggested to be the rate-determining step, and thus Serotonin N-acetyltransferase has ... Aralkylamine N-acetyltransferase (AANAT) (EC 2.3.1.87), also known as arylalkylamine N-acetyltransferase or serotonin N- ... Aralkylamine N-acetyltransferase belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily which consists 10,000 ... Other well-studied members of the superfamily are glucosamine-6-phosphate N-acetyltransferase and histone acetyltransferases. ...
*  Glutamate N-acetyltransferase
... ornithine acetyltransferase, and 2-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase. This enzyme participates in urea cycle ... acetylornithine glutamate acetyltransferase, glutamate acetyltransferase, N-acetyl-L-glutamate synthetase, N-acetylglutamate ... The systematic name of this enzyme class is N2-acetyl-L-ornithine:L-glutamate N-acetyltransferase. Other names in common use ... In enzymology, a glutamate N-acetyltransferase (EC 2.3.1.35) is an enzyme that catalyzes the chemical reaction N2-acetyl-L- ...
*  Alcohol O-acetyltransferase
In enzymology, an alcohol O-acetyltransferase (EC 2.3.1.84) is an enzyme that catalyzes the chemical reaction acetyl-CoA + an ... The systematic name of this enzyme class is acetyl-CoA:alcohol O-acetyltransferase. This enzyme is also called alcohol ... Yoshioka K; Hashimoto N (1981). "Ester formation by alcohol acetyltransferase from brewers' yeast". Agric. Biol. Chem. 45: 2183 ...
*  Leucine N-acetyltransferase
In enzymology, a leucine N-acetyltransferase (EC 2.3.1.66) is an enzyme that catalyzes the chemical reaction acetyl-CoA + L- ... The systematic name of this enzyme class is acetyl-CoA:L-leucine N-acetyltransferase. This enzyme is also called leucine ... acetyltransferase. Suzukake S, Hayashi H, Hori M, Umezawa H (1982). "Biosnthesis of leupeptin III. Isolation and properties of ...
*  Aminoglycoside N6'-acetyltransferase
... acetyltransferase, aminoglycoside-6-N-acetyltransferase, and kanamycin acetyltransferase. As of late 2007, 4 structures have ... The systematic name of this enzyme class is acetyl-CoA:kanamycin-B N6'-acetyltransferase. Other names in common use include ... In enzymology, an aminoglycoside N6'-acetyltransferase (EC 2.3.1.82) is an enzyme that catalyzes the chemical reaction acetyl- ... Le Goffic F, Martel A (1974). "[Resistance to aminosides induced by an isoenzyme, kanamycin acetyltransferase]". Biochimie. 56 ...
*  Serine O-acetyltransferase
Other names in common use include SATase, L-serine acetyltransferase, serine acetyltransferase, and serine transacetylase. This ... In enzymology, a serine O-acetyltransferase (EC 2.3.1.30) is an enzyme that catalyzes the chemical reaction acetyl-CoA + L- ... In molecular biology, the protein domain SATase is short for Serine acetyltransferase and refers to an enzyme that catalyses ... Of particular interest to scientists, is the ability to harness the natural ability of the enzyme, Serine acetyltransferase, to ...
*  Imidazole N-acetyltransferase
In enzymology, an imidazole N-acetyltransferase (EC 2.3.1.2) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... The systematic name of this enzyme class is acetyl-CoA:imidazole N-acetyltransferase. Other names in common use include ... imidazole acetylase, and imidazole acetyltransferase. Kinsky SC (1960). "Assay, purification, and properties of imidazole ...
*  Histidine N-acetyltransferase
In enzymology, a histidine N-acetyltransferase (EC 2.3.1.33) is an enzyme that catalyzes the chemical reaction acetyl-CoA + L- ... The systematic name of this enzyme class is acetyl-CoA:L-histidine N-acetyltransferase. Other names in common use include ... acetylhistidine synthetase, and histidine acetyltransferase. Baslow MH (1966). "N -acetyl-L-histidine synthetase activity from ...
*  Glucosamine N-acetyltransferase
In enzymology, a glucosamine N-acetyltransferase (EC 2.3.1.3) is an enzyme that catalyzes the chemical reaction acetyl-CoA + D- ... The systematic name of this enzyme class is acetyl-CoA:D-glucosamine N-acetyltransferase. Other names in common use include ... glucosamine acetylase, and glucosamine acetyltransferase. This enzyme participates in aminosugars metabolism. CHOU TC, SOODAK M ...
*  Phenylalanine N-acetyltransferase
The systematic name of this enzyme class is acetyl-CoA:L-phenylalanine N-acetyltransferase. This enzyme is also called acetyl- ... In enzymology, a phenylalanine N-acetyltransferase (EC 2.3.1.53) is an enzyme that catalyzes the chemical reaction acetyl-CoA ... CoA-L-phenylalanine alpha-N-acetyltransferase. This enzyme participates in phenylalanine metabolism. Leuzinger W, Baker AL, ...
Study finds N-alpha-acetyltransferase D (NatD) promotes lung cancer progression | EurekAlert! Science News  Study finds N-alpha-acetyltransferase D (NatD) promotes lung cancer progression | EurekAlert! Science News
Study finds N-alpha-acetyltransferase D (NatD) promotes lung cancer progression. Nanjing University School of Life Sciences ...
more infohttps://eurekalert.org/pub_releases/2017-10/nuso-sfn101217.php
Connecting the histone acetyltransferase complex SAS-I to the centromere in S. cerevisiae  Connecting the histone acetyltransferase complex SAS-I to the centromere in S. cerevisiae
... über seinen einzigartigen N-Terminus mit zwei Komponenten des Histon-Acetyltransferase-Komplexes SAS-I interagiert: der ... that the histone H3 variant was able to interact over its unique N-Terminus with two subunits of the histone acetyltransferase ...
more infohttps://edoc.hu-berlin.de/handle/18452/15787
Plus it  Plus it
Arylamine N-Acetyltransferase 1: A Novel Drug Target in Cancer Development. Neville J. Butcher and Rodney F. Minchin ... Arylamine N-Acetyltransferase 1: A Novel Drug Target in Cancer Development. Neville J. Butcher and Rodney F. Minchin ... Arylamine N-Acetyltransferase 1: A Novel Drug Target in Cancer Development. Neville J. Butcher and Rodney F. Minchin ... Arylamine N-Acetyltransferase 1: A Novel Drug Target in Cancer Development Message Subject (Your Name) has forwarded a page to ...
more infohttp://pharmrev.aspetjournals.org/content/early/2011/11/14/pr.110.004275
IJMS  | Free Full-Text | In Silico Identification and Characterization of N-Terminal Acetyltransferase Genes of Poplar (Populus...  IJMS | Free Full-Text | In Silico Identification and Characterization of N-Terminal Acetyltransferase Genes of Poplar (Populus...
N-terminal acetyltransferase (Nats) complex is responsible for protein N-terminal acetylation (Nα-acetylation), which is one of ... N-terminal acetyltransferase (Nats) complex is responsible for protein N-terminal acetylation (Nα-acetylation), which is one of ... Hollebeke, J.; van Damme, P.; Gevaert, K. N-terminal acetylation and other functions of N-α-acetyltransferases. Biol. Chem 2012 ... Table 1. All identified N-terminal acetyltransferase (Nat) genes (CS and AS) and putative encoded poplypeptides present in ...
more infohttp://www.mdpi.com/1422-0067/15/2/1852/htm
N-Acetyltransferase-2 (NAT2) gene polymorphisms and enzyme activity in Serbs: unprecedented high prevalence of rapid...  N-Acetyltransferase-2 (NAT2) gene polymorphisms and enzyme activity in Serbs: unprecedented high prevalence of rapid...
N-Acetyltransferase-2 (NAT2) gene polymorphisms and enzyme activity in Serbs: unprecedented high prevalence of rapid ... The aim of this study was to investigate N-acetyltransferase 2 (NAT2) genetic polymorphism and enzyme activity in Serbs, and to ...
more infohttps://www.sigmaaldrich.com/catalog/papers/20801937
N-Acetyltransferase activity in cultured-cells  - Kingston University Research Repository  N-Acetyltransferase activity in cultured-cells - Kingston University Research Repository
Christie, Angela, Burgess, Anne P. and Sim, Edith (1987) N-Acetyltransferase activity in cultured-cells. Biochemical Society ...
more infohttp://eprints.kingston.ac.uk/19428/
Mouse N-acetyltransferase type 2, the homologue of human N-acetyltransferase type 1. - Oxford Neuroscience  Mouse N-acetyltransferase type 2, the homologue of human N-acetyltransferase type 1. - Oxford Neuroscience
There is increasing evidence that human arylamine N-acetyltransferase type 1 (NAT1, EC 2.3.1.5), although first identified as a ... Mouse N-acetyltransferase type 2, the homologue of human N-acetyltransferase type 1. ... Mouse N-acetyltransferase type 2, the homologue of human N-acetyltransferase type 1. ... There is increasing evidence that human arylamine N-acetyltransferase type 1 (NAT1, EC 2.3.1.5), although first identified as a ...
more infohttps://www.neuroscience.ox.ac.uk/publications/100011
Atomic resolution structure of human alpha-tubulin acetyltransferase
   bound to acetyl-CoA :: MPG.PuRe
				  Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA :: MPG.PuRe
Atomic resolution structure of human alpha-tubulin acetyltransferase,br/, bound to acetyl-CoA ... Compared with other lysine acetyltransferases of known structure, alpha-tubulin acetyltransferase displays a relatively well- ... Whereas histone acetyltransferases have been extensively studied, there is no structural and mechanistic information available ... Taschner, M., Vetter, M., & Lorentzen, E. (2012). Atomic resolution structure of human alpha-tubulin acetyltransferase bound to ...
more infohttp://pubman.mpdl.mpg.de/pubman/faces/viewItemOverviewPage.jsp?itemId=escidoc:1609330
Functional characterization of single-nucleotide polymorphisms and haplotypes of human N-acetyltransferase 2 : Carcinogenesis -...  Functional characterization of single-nucleotide polymorphisms and haplotypes of human N-acetyltransferase 2 : Carcinogenesis -...
Human N-acetyltransferase 2 (NAT2) is polymorphic in humans and may associate with cancer risk by modifying individual ... Human N-acetyltransferase 2 (NAT2) is polymorphic in humans and may associate with cancer risk by modifying individual ...
more infohttp://oxfordindex.oup.com/view/10.1093/carcin/bgm085
A novel human NatA Nα-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1) | BMC Biochemistry | Full Text  A novel human NatA Nα-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1) | BMC Biochemistry | Full Text
... histone acetyltransferases) and co-translational Nα-terminal acetylation catalyzed by NATs (N-terminal acetyltransferases). The ... N-terminal acetyltransferase activity of the hNaa16p-hNaa10p complex. HeLa cells were transfected with phNAA16-FLAG and phNAA10 ... In vitro Nα-acetyltransferase assay. HEK293 cells were transfected by plasmids as described above and indicated in Figure 8, ... Arnesen T, Gromyko D, Horvli O, Fluge O, Lillehaug J, Varhaug JE: Expression of N-acetyl transferase human and human Arrest ...
more infohttps://bmcbiochem.biomedcentral.com/articles/10.1186/1471-2091-10-15
The MYST family histone acetyltransferase complex regulates stress resistance and longevity through transcriptional control of...  The MYST family histone acetyltransferase complex regulates stress resistance and longevity through transcriptional control of...
Here, we report an unexpected finding that the MYST family histone acetyltransferase complex (MYS‐1/TRR‐1 complex) promotes ... Our results thus identify the evolutionarily conserved role of the MYST family acetyltransferase as a key epigenetic regulator ... The MYST family histone acetyltransferase complex regulates stress resistance and longevity through transcriptional control of ...
more infohttp://embor.embopress.org/content/18/10/1716
The MYST family histone acetyltransferase complex regulates stress resistance and longevity through transcriptional control of...  The MYST family histone acetyltransferase complex regulates stress resistance and longevity through transcriptional control of...
Here, we report an unexpected finding that the MYST family histone acetyltransferase complex (MYS‐1/TRR‐1 complex) promotes ... Our results thus identify the evolutionarily conserved role of the MYST family acetyltransferase as a key epigenetic regulator ... The MYST family histone acetyltransferase complex regulates stress resistance and longevity through transcriptional control of ...
more infohttp://embor.embopress.org/content/early/2017/08/09/embr.201743907
LongevityMap variant  LongevityMap variant
N-acetyltransferase 2 Description. This gene encodes an enzyme that functions to both activate and deactivate arylamine and ... A second arylamine N-acetyltransferase gene (NAT1) is located near this gene (NAT2). [provided by RefSeq, Jul 2008]. Other ...
more infohttp://genomics.senescence.info/longevity/entry.php?id=23
Histone acetyltransferases.  - PubMed - NCBI  Histone acetyltransferases. - PubMed - NCBI
This review discusses our current understanding of histone acetyltransferases (HATs) or acetyltransferases (ATs): their ... Histone acetyltransferases.. Roth SY1, Denu JM, Allis CD.. Author information. 1. Department of Biochemistry and Molecular ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/11395403?dopt=Abstract
Histone acetyltransferase - Wikipedia  Histone acetyltransferase - Wikipedia
Acetyltransferase. References[edit]. *^ a b c d e f g h i Lee KK, Workman JL (April 2007). "Histone acetyltransferase complexes ... Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring ... Gcn5-related N-acetyltransferases (GNATs)[edit]. HATs can be grouped into several different families based on sequence homology ... The Gcn5-related N-acetyltransferase (GNAT) family includes Gcn5, PCAF, Hat1, Elp3, Hpa2, Hpa3, ATF-2, and Nut1. These HATs are ...
more infohttps://en.wikipedia.org/wiki/Histone_acetyltransferase
Structure of histone acetyltransferases.  - PubMed - NCBI  Structure of histone acetyltransferases. - PubMed - NCBI
Structure of histone acetyltransferases.. Marmorstein R1.. Author information. 1. The Wistar Institute and the Department of ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/11492997?dopt=Abstract
Browsing University Archives by Subject Acetyltransferases -- Purification  Browsing University Archives by Subject "Acetyltransferases -- Purification"
Isolation, partial purification and characterization of an N-acetyltransferase from Streptomyces akiyoshiensis L-138  ...
more infohttps://www.uleth.ca/dspace/handle/10133/1/browse?value=Acetyltransferases+--+Purification&type=subject
Diamine acetyltransferase 1 (IPR032957) | InterPro | EMBL-EBI  Diamine acetyltransferase 1 (IPR032957) | InterPro | EMBL-EBI
Diamine acetyltransferase 1, also known as spermidine/spermine-N(1)-acetyltransferase (SSAT), is an enzyme that catalyses the ... GO:0004145 diamine N-acetyltransferase activity GO:0005515 protein binding Cellular Component. No terms assigned in this ... Spermidine/spermine-N(1)-acetyltransferase: a key metabolic regulator.. Am. J. Physiol. Endocrinol. Metab. 294 E995-1010 2008 ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR032957
Dysregulation of Histone Acetyltransferases and Deacetylases in Cardiovascular Diseases  Dysregulation of Histone Acetyltransferases and Deacetylases in Cardiovascular Diseases
... Yonggang Wang,1,2 Xiao Miao,2,3 ... X. Yang, W. Yu, L. Shi et al., "HAT4, a golgi apparatus-anchored B-type histone acetyltransferase, acetylates free histone H4 ... D. Cao, Z. Wang, C.-L. Zhang et al., "Modulation of smooth muscle gene expression by association of histone acetyltransferases ... M. R. Parthun, J. Widom, and D. E. Gottschling, "The major cytoplasmic histone acetyltransferase in yeast: links to chromatin ...
more infohttps://www.hindawi.com/journals/omcl/2014/641979/ref/
Arylamine N-acetyltransferases 3 | HSTalks  Arylamine N-acetyltransferases 3 | HSTalks
Edith Sim on Arylamine N-acetyltransferases 3, part of a collection of online lectures. ... Arylamine N-acetyltransferases. Part 3 I'm Edith Sim, and I have been working on these enzymes for over 20 years. ... Sim, E. (2016, July 28). Arylamine N-acetyltransferases 3 [Video file]. In The Biomedical & Life Sciences Collection, Henry ... Arylamine N-acetyltransferases 3. Part 3 of 3 *Part 1 of 3 ... Arylamine N-acetyltransferases (recap). *Nat in fungi ...
more infohttps://hstalks.com/t/3320/arylamine-n-acetyltransferases-3/?biosci