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.Hemoglobins: The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.Aspirin: The prototypical analgesic used in the treatment of mild to moderate pain. It has anti-inflammatory and antipyretic properties and acts as an inhibitor of cyclooxygenase which results in the inhibition of the biosynthesis of prostaglandins. Aspirin also inhibits platelet aggregation and is used in the prevention of arterial and venous thrombosis. (From Martindale, The Extra Pharmacopoeia, 30th ed, p5)Hemoglobin A: Normal adult human hemoglobin. The globin moiety consists of two alpha and two beta chains.Oxyhemoglobins: A compound formed by the combination of hemoglobin and oxygen. It is a complex in which the oxygen is bound directly to the iron without causing a change from the ferrous to the ferric state.Hemoglobins, Abnormal: Hemoglobins characterized by structural alterations within the molecule. The alteration can be either absence, addition or substitution of one or more amino acids in the globin part of the molecule at selected positions in the polypeptide chains.Biological Products: Complex pharmaceutical substances, preparations, or matter derived from organisms usually obtained by biological methods or assay.CarboxyhemoglobinAccess to Information: Individual's rights to obtain and use information collected or generated by others.BoliviaEcuadorBiotechnology: Body of knowledge related to the use of organisms, cells or cell-derived constituents for the purpose of developing products which are technically, scientifically and clinically useful. Alteration of biologic function at the molecular level (i.e., GENETIC ENGINEERING) is a central focus; laboratory methods used include TRANSFECTION and CLONING technologies, sequence and structure analysis algorithms, computer databases, and gene and protein structure function analysis and prediction.Moraceae: The mulberry plant family of the order Urticales, subclass Hamamelidae, class Magnoliopsida. They have milky latex and small, petalless male or female flowers.BrazilCaliforniaGenomics: The systematic study of the complete DNA sequences (GENOME) of organisms.Flow Cytometry: Technique using an instrument system for making, processing, and displaying one or more measurements on individual cells obtained from a cell suspension. Cells are usually stained with one or more fluorescent dyes specific to cell components of interest, e.g., DNA, and fluorescence of each cell is measured as it rapidly transverses the excitation beam (laser or mercury arc lamp). Fluorescence provides a quantitative measure of various biochemical and biophysical properties of the cell, as well as a basis for cell sorting. Other measurable optical parameters include light absorption and light scattering, the latter being applicable to the measurement of cell size, shape, density, granularity, and stain uptake.Databases, Genetic: Databases devoted to knowledge about specific genes and gene products.Botany: The study of the origin, structure, development, growth, function, genetics, and reproduction of plants.Sirtuin 3: A sirtuin family member found primarily in MITOCHONDRIA. It is a multifunctional enzyme that contains a NAD-dependent deacetylase activity that is specific for HISTONES and a mono-ADP-ribosyltransferase activity.Acetyltransferases: Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.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.Histone Acetyltransferases: Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.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.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.Host-Pathogen Interactions: The interactions between a host and a pathogen, usually resulting in disease.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)alpha Karyopherins: Nucleocytoplasmic transport molecules that bind to the NUCLEAR LOCALIZATION SIGNALS of cytoplasmic molecules destined to be imported into the CELL NUCLEUS. Once attached to their cargo they bind to BETA KARYOPHERINS and are transported through the NUCLEAR PORE COMPLEX. Inside the CELL NUCLEUS alpha karyopherins dissociate from beta karypherins and their cargo. They then form a complex with CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN and RAN GTP-BINDING PROTEIN which is exported to the CYTOPLASM.beta Karyopherins: Nucleocytoplasmic transport molecules that bind to ALPHA KARYOPHERINS in the CYTOSOL and are involved in transport of molecules through the NUCLEAR PORE COMPLEX. Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. Beta karyopherins bound to RAN GTP-BINDING PROTEIN are then re-transported to the cytoplasm where hydrolysis of the GTP of RAN GTP-BINDING PROTEIN causes release of karyopherin beta.Pepsin A: Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.Phenol: An antiseptic and disinfectant aromatic alcohol.Tyrosine: A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Pepsinogens: Proenzymes secreted by chief cells, mucous neck cells, and pyloric gland cells, which are converted into pepsin in the presence of gastric acid or pepsin itself. (Dorland, 28th ed) In humans there are 2 related pepsinogen systems: PEPSINOGEN A (formerly pepsinogen I or pepsinogen) and PEPSINOGEN C (formerly pepsinogen II or progastricsin). Pepsinogen B is the name of a pepsinogen from pigs.Focus Groups: A method of data collection and a QUALITATIVE RESEARCH tool in which a small group of individuals are brought together and allowed to interact in a discussion of their opinions about topics, issues, or questions.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.Kinetics: The rate dynamics in chemical or physical systems.Lysine: An essential amino acid. It is often added to animal feed.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.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.Heterochromatin: The portion of chromosome material that remains condensed and is transcriptionally inactive during INTERPHASE.
(1/6505) UK-18892, a new aminoglycoside: an in vitro study.

UK-18892 is a new aminoglycoside antibiotic, a derivative of kanamycin A structurally related to amikacin. It was found to be active against a wide range of pathogenic bacteria, including many gentamicin-resistant strains. The spectrum and degree of activity of UK-18892 were similar to those of amikacin, and differences were relatively minor. UK-18892 was about twice as active as amikacin against gentamicin-susceptible strains of Pseudomonas aeruginosa. Both amikacin and UK-18892 were equally active against gentamicin-resistant strains of P. aeruginosa. There were no appreciable differences in the activity of UK-18892 and amikacin against Enterobacteriaceae and Staphylococcus aureus. Cross-resistance between these two antimicrobials was also apparent.  (+info)

(2/6505) 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)

(3/6505) Probing interactions between HIV-1 reverse transcriptase and its DNA substrate with backbone-modified nucleotides.

BACKGROUND: To gain a molecular understanding of a biochemical process, the crystal structure of enzymes that catalyze the reactions involved is extremely helpful. Often the question arises whether conformations obtained in this way appropriately reflect the reactivity of enzymes, however. Rates that characterize transitions are therefore compulsory experiments for the elucidation of the reaction mechanism. Such experiments have been performed for the reverse transcriptase of the type 1 human immunodeficiency virus (HIV-1 RT). RESULTS: We have developed a methodology to monitor the interplay between HIV-1 RT and its DNA substrate. To probe the protein-DNA interactions, the sugar backbone of one nucleotide was modified by a substituent that influenced the efficiency of the chain elongation in a characteristic way. We found that strand elongation after incorporation of the modified nucleotide follows a discontinuous efficiency for the first four nucleotides. The reaction efficiencies could be correlated with the distance between the sugar substituent and the enzyme. The model was confirmed by kinetic experiments with HIV-1 RT mutants. CONCLUSIONS: Experiments with HIV-1 RT demonstrate that strand-elongation efficiency using a modified nucleotide correlates well with distances between the DNA substrate and the enzyme. The functional group at the modified nucleotides acts as an 'antenna' for steric interactions that changes the optimal transition state. Kinetic experiments in combination with backbone-modified nucleotides can therefore be used to gain structural information about reverse transcriptases and DNA polymerases.  (+info)

(4/6505) High-throughput screening of small molecules in miniaturized mammalian cell-based assays involving post-translational modifications.

BACKGROUND: Fully adapting a forward genetic approach to mammalian systems requires efficient methods to alter systematically gene products without prior knowledge of gene sequences, while allowing for the subsequent characterization of these alterations. Ideally, these methods would also allow function to be altered in a temporally controlled manner. RESULTS: We report the development of a miniaturized cell-based assay format that enables a genetic-like approach to understanding cellular pathways in mammalian systems using small molecules, rather than mutations, as the source of gene-product alterations. This whole-cell immunodetection assay can sensitively detect changes in specific cellular macromolecules in high-density arrays of mammalian cells. Furthermore, it is compatible with screening large numbers of small molecules in nanoliter to microliter culture volumes. We refer to this assay format as a 'cytoblot', and demonstrate the use of cytoblotting to monitor biosynthetic processes such as DNA synthesis, and post-translational processes such as acetylation and phosphorylation. Finally, we demonstrate the applicability of these assays to natural-product screening through the identification of marine sponge extracts exhibiting genotype-specific inhibition of 5-bromodeoxyuridine incorporation and suppression of the anti-proliferative effect of rapamycin. CONCLUSIONS: We show that cytoblots can be used for high-throughput screening of small molecules in cell-based assays. Together with small-molecule libraries, the cytoblot assay can be used to perform chemical genetic screens analogous to those used in classical genetics and thus should be applicable to understanding a wide variety of cellular processes, especially those involving post-transitional modifications.  (+info)

(5/6505) 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)

(6/6505) 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)

(7/6505) Gibberellic acid stabilises microtubules in maize suspension cells to cold and stimulates acetylation of alpha-tubulin.

Gibberellic acid is known to stabilise microtubules in plant organs against depolymerisation. We have now devised a simplified cell system for studying this. Pretreatment of a maize cell suspension with gibberellic acid for just 3 h stabilised protoplast microtubules against depolymerisation on ice. In other eukaryotes, acetylation of alpha-tubulin is known to correlate with microtubule stabilisation but this is not established in plants. By isolating the polymeric tubulin fraction from maize cytoskeletons and immunoblotting with the antibody 6-11B-1, we have demonstrated that gibberellic acid stimulates the acetylation of alpha-tubulin. This is the first demonstrated link between microtubule stabilisation and tubulin acetylation in higher plants.  (+info)

(8/6505) Expanded lysine acetylation specificity of Gcn5 in native complexes.

The coactivator/adaptor protein Gcn5 is a conserved histone acetyltransferase, which functions as the catalytic subunit in multiple yeast transcriptional regulatory complexes. The ability of Gcn5 to acetylate nucleosomal histones is significantly reduced relative to its activity on free histones, where it predominantly modifies histone H3 at lysine 14. However, the association of Gcn5 in multisubunit complexes potentiates its nucleosomal histone acetyltransferase activity. Here, we show that the association of Gcn5 with other proteins in two native yeast complexes, Ada and SAGA (Spt-Ada-Gcn5-acetyltransferase), directly confers upon Gcn5 the ability to acetylate an expanded set of lysines on H3. Furthermore Ada and SAGA have overlapping, yet distinct, patterns of acetylation, suggesting that the association of specific subunits determines site specificity.  (+info)

*  Acetylation
The lysine acetylation of STAT3 is also elevated in cancer cells. Since the acetylation of STAT3 is important for its oncogenic ... The acetylation of p53 is indispensable for its activation. It has been reported that the acetylation level of p53 will ... "Protein Acetylation: Much More than Histone Acetylation". Cayman Chemical. Archived from the original on 2014-02-28. Zhao S, Xu ... There are three major acetylation sites on p53: K164, K120 and C terminus. If only one of the acetylation sites is defected, ...
*  Histone acetylation and deacetylation
The acetylation pattern is regulated by HAT and HADC enzymes and, in turn, sets the local chromatin structure. In this way, ... Acetylation is the process where an acetyl functional group is transferred from one molecule (in this case, Acetyl-Coenzyme A) ... Acetylation has the effect of changing the overall charge of the histone tail from positive to neutral. Nucleosome formation is ... Acetylation removes the positive charge on the histones, thereby decreasing the interaction of the N termini of histones with ...
*  Compendium of protein lysine acetylation
The compendium of protein lysine acetylation (CPLA) database contains the sites of experimentally identified lysine acetylation ... an integrated database of protein lysine acetylation". Nucleic Acids Res. England. 39 (Database issue): D1029-34. doi:10.1093/ ...
*  EHD3
The EHD3 protein suffers three kinds of amino acid modifications: Acetylation. It consists of attaching an acetyl group at the ... "Acetylation". www.uniprot.org. Retrieved 2016-10-16. Chukkapalli, Sahiti; Amessou, Mohamed; Dekhil, Hafedh; Dilly, Ashok Kumar ...
*  Acetoacetate decarboxylase
Selective acetylation of enzyme". Biochemistry. 7 (3): 913-919. doi:10.1021/bi00843a005. Schmidt, Donald E.; F.H. Westheimer ( ...
*  Post-translational modification
See also histone acetylation. The reverse is called deacetylation. formylation alkylation, the addition of an alkyl group, e.g ... Polevoda B, Sherman F; Sherman (2003). "N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of ... Yang XJ, Seto E; Seto (2008). "Lysine acetylation: codified crosstalk with other posttranslational modifications". Mol Cell. 31 ... acetylation, the addition of an acetyl group, either at the N-terminus of the protein or at lysine residues. ...
*  GCN5L2
Col E, Gilquin B, Caron C, Khochbin S (2002). "Tat-controlled protein acetylation". J. Biol. Chem. 277 (40): 37955-60. doi: ... Randhawa GS, Bell DW, Testa JR, Feinberg AP (1998). "Identification and mapping of human histone acetylation modifier gene ... "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. 20 (12): ... "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. 20 (12): ...
*  Arylamine N-acetyltransferase
Tabor H, Mehler AH, Stadtman ER (1953). "The enzymatic acetylation of amines". J. Biol. Chem. 204 (1): 127-138. PMID 13084583. ... Weissbach H, Redfield BG, Axelrod J (1961). "The enzymic acetylation of serotonin and other naturally occurring amines". ...
*  Carnitine O-acetyltransferase
Friedman S, Fraenkel G (Dec 1955). "Reversible enzymatic acetylation of carnitine". Archives of Biochemistry and Biophysics. 59 ...
*  Alpha-tubulin N-acetyltransferase
Tubulin acetylation is one of the signaling pathways for Na+ and K+-ATPase activity. Tubulin acetylation is also involved in ... Tubulin acetylation by ATAT1 has been shown to be elevated by the cell exposure to UV irradiation, as well as its exposure to ... The acetylation is used y the cell as a marker for these stable microtubules. ATAT1 specifically acetylates 'Lys-40' in alpha ... There are some cases in which the mutation of the gene might cause a reduction in the acetylation of the microtubules. Like for ...
*  HIST1H4I
Turner BM, O'Neill LP, Allan IM (1989). "Histone H4 acetylation in human cells. Frequency of acetylation at different sites ... 2001). "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core ... Lusic M, Marcello A, Cereseto A, Giacca M (2004). "Regulation of HIV-1 gene expression by histone acetylation and factor ...
*  FAM149A
NetAcet: Predicts N-terminal acetylation sites. Here are the results: According to NetAcet, there are no N-terminal acetylation ...
*  Acetyl-CoA
This acetylation is catalyzed by acetyltransferases. This acetylation affects cell growth, mitosis, and apoptosis. Allosteric ... Melatonin synthesis Acetylation Acetyl-CoA is also the source of the acetyl group incorporated onto certain lysine residues of ... Fritz Lipmann won the Nobel Prize in 1953 for his discovery of the cofactor coenzyme A. The acetylation of CoA is determined by ... Ethanol also serves as a carbon source for acetylation of CoA utilizing the enzyme alcohol dehydrogenase. Degradation of ...
*  Histrionicotoxins
Hydrolysis, reduction and acetylation yielded 136. Formation of a thiolactam followed by condensation with ethyl bromoacetate ...
*  Chromatin remodeling
Acetylation - by HAT (histone acetyl transferase); deacetylation - by HDAC (histone deacetylase) Acetylation tends to define ... On contrary, histone acetylation relaxes chromatin condensation and exposes DNA for TF binding, leading to increase gene ... These enzymatic modifications include acetylation, methylation, phosphorylation, and ubiquitination and primarily occur at N- ... "Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation". Proceedings of ...
*  Histone code
Acetylation - by HAT (histone acetyl transferase); deacetylation - by HDAC (histone deacetylase) Acetylation tends to define ... Similarly, the combination of phosphorylation of serine residue 10 and acetylation of a lysine residue 14 on histone H3 is a ... Liang, G (2004). "Distinct localization of histone H3 acetylation and H3-K4 methylation to the transcription start sites in the ... 2008). "Combinatorial patterns of histone acetylations and methylations in the human genome". Nat Genet. 40 (7): 897-903. doi: ...
*  PCAF
Ott M, Dorr A, Hetzer-Egger C, Kaehlcke K, Schnolzer M, Henklein P, Cole P, Zhou MM, Verdin E (2004). "Tat acetylation: a ... Acetylation leads to migration to the nucleus and enhances its acetyltransferase activity. PCAF interacts with and is ... PCAF also possesses sites for its own acetylation and ubiquitination. CBP and p300 are large nuclear proteins that bind to many ... The acetyltransferase activity and cellular location of PCAF are regulated through acetylation of PCAF itself. PCAF may be ...
*  Systems biology
i.e., DNA methylation, Histone acetylation and deacetylation, etc.). Transcriptomics Organismal, tissue or whole cell gene ...
*  SUHW4
The glycine residue at position 2 is a probable candidate for N-terminal acetylation. There are seven probable sumoylation ... "NetAcet: Prediction of N-terminal acetylation sites". NetAcet. Retrieved 7 May 2014. "SUMOplot™ Analysis Program". Retrieved 7 ...
*  Tetrahymena
Demonstration of the roles of posttranslational modification such as acetylation and glycylation on tubulins and discovery of ... Discovery of the function of histone acetylation. ...
*  CCDC130
Kiemer L, Bendtsen JD, Blom N (2005). "NetAcet: prediction of N-terminal acetylation sites". Bioinformatics (Oxford, England). ...
*  Histone acetyltransferase
This acetylation pattern has been seen during histone synthesis. Another example is acetylation of H4K16, which has been ... However, acetylation is not always associated with enhanced transcriptional activity. For instance, acetylation of H4K12 has ... In general, histone acetylation increases gene expression. In general, histone acetylation is linked to transcriptional ... In flies, acetylation of H4K16 on the male X chromosome by MOF in the context of the MSL complex is correlated with ...
*  Salt End
"BP marks 50 years in Hull; supports creation of a wood acetylation consortium , Press releases and latest news , Media , United ...
*  ING1
"DNA damage-inducible gene p33ING2 negatively regulates cell proliferation through acetylation of p53". Proceedings of the ... "Human ING1 proteins differentially regulate histone acetylation". The Journal of Biological Chemistry. 277 (33): 29832-9. doi: ...
*  Acetyltributylcitrate
It is prepared by acetylation of tributylcitrate. Britt E. Erickson: Regulators And Retailers Raise Pressure On Phthalates, ...
Acetylation - Wikipedia  Acetylation - Wikipedia
The lysine acetylation of STAT3 is also elevated in cancer cells. Since the acetylation of STAT3 is important for its oncogenic ... The acetylation of p53 is indispensable for its activation. It has been reported that the acetylation level of p53 will ... "Protein Acetylation: Much More than Histone Acetylation". Cayman Chemical. Archived from the original on 2014-02-28. Zhao S, Xu ... There are three major acetylation sites on p53: K164, K120 and C terminus. If only one of the acetylation sites is defected, ...
more infohttps://en.wikipedia.org/wiki/Acetylation
Histone acetylation and deacetylation - Wikipedia  Histone acetylation and deacetylation - Wikipedia
The acetylation pattern is regulated by HAT and HADC enzymes and, in turn, sets the local chromatin structure. In this way, ... Acetylation is the process where an acetyl functional group is transferred from one molecule (in this case, Acetyl-Coenzyme A) ... Acetylation has the effect of changing the overall charge of the histone tail from positive to neutral. Nucleosome formation is ... Acetylation removes the positive charge on the histones, thereby decreasing the interaction of the N termini of histones with ...
more infohttps://en.wikipedia.org/wiki/Histone_acetylation_and_deacetylation
Acetylation | The Scientist Magazine®  Acetylation | The Scientist Magazine®
Acetylation. Acetylation. In March 1996, a laboratory from the University of Rochester announced the discovery of an enzyme ... Now probably acetylation is one of the hottest topics in gene regulation.'. Allis's lab succeeded in purifying a nuclear HAT ... Histone proteins have been known for years to be marked by other modifications besides acetylation, such as methylation, ... a homolog to yeast Gcn5p linking histone acetylation to gene activation,' Cell, 84:843-851, 1996. (Cited in more than 250 ...
more infohttps://the-scientist.com/hot-paper/acetylation-56606/amp
What Is Acetylation? (with pictures)  What Is Acetylation? (with pictures)
Acetylation is the process of adding an acetyl radical to a protein while a hydrogen atoms leaves it so that an acetate is ... Acetylation is one of the most studied processes in epigenetics. If proteins can control how DNA is replicated and the amount ... For acetylation to occur, N-alpha-acetyltransferases have to be present. There are three common variations of these that are ... There is a way acetylation is triggered by cellular proteins and when the reaction begins, chemicals are added to the DNA- ...
more infohttps://www.wisegeek.com/what-is-acetylation.htm
Mitochondrial Acetylation and Diseases of Aging  Mitochondrial Acetylation and Diseases of Aging
3. Nε-Acetylation. Acetylation occurring on the epsilon-amino group of lysine residues (. -acetylation) was discovered on ... Constitutively mimicking de-acetylation at K42 induced a nearly 60% increase in LCAD activity. Furthermore, acetylation at only ... acetylation focused almost exclusively on histone substrates [21-23]. It was not until 1996 that Taunton et al. purified the ... Mitochondrial acetylation biology is an infant field of study that, in the future, will have the potential to bridge our ...
more infohttps://www.hindawi.com/journals/jar/2011/234875/
Acetylation control of cancer cell metabolism.  - PubMed - NCBI  Acetylation control of cancer cell metabolism. - PubMed - NCBI
Acetylation control of cancer cell metabolism.. Lin R, Zhou X, Huang W, Zhao D, Lv L, Xiong Y, Guan KL, Lei QY1. ... Lysine acetylation plays an essential role in metabolism. Five individual studies have identified that a large number of ... the dysfunction of acetylation regulation in tumorigenesis and their potential role in cancer metabolism therapy. ... This review focuses on recent advances in the acetylation regulation of metabolic enzymes involved in the Warburg effect, ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/23859620?dopt=Abstract
Protein Acetylation in Archaea, Bacteria, and Eukaryotes  Protein Acetylation in Archaea, Bacteria, and Eukaryotes
For N-terminal acetylation in Drosophila, the (X)PX-rule (proline at first or second position inhibits acetylation) was used to ... It remains to be clarified whether differential histone acetylation is essential for H. volcanii or whether the acetylation of ... In contrast to eukaryotes, acetylation in E. coli occurs posttranslationally. Acetylation of S12 has been shown to stablize the ... The reason why the degree of N-terminal acetylation was overlooked for so long is probably that the acetylation typically is ...
more infohttps://www.hindawi.com/journals/archaea/2010/820681/
Metabolic Regulation Through Acetylation | Science Signaling  Metabolic Regulation Through Acetylation | Science Signaling
Control of metabolism by acetylation appears to be evolutionarily conserved: Wang et al. found that the ability of the ... Acetylation regulated various enzymes by distinct mechanisms, directly activating some, inhibiting one, and controlling the ... Now, two papers suggest that acetylation may represent an important regulatory mechanism controlling the function of metabolic ... Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 327, 1004-1007 (2010). [ ...
more infohttps://stke.sciencemag.org/content/3/110/ec59.abstract
Histone acetylation: molecular mnemonics on the chromatin.  - PubMed - NCBI  Histone acetylation: molecular mnemonics on the chromatin. - PubMed - NCBI
Histone acetylation: molecular mnemonics on the chromatin.. Gräff J1, Tsai LH. ... As histone acetylation and cognitive functions can be pharmacologically restored by histone deacetylase inhibitors, this ... Whereas increments in histone acetylation have consistently been shown to favour learning and memory, a lack thereof has been ... Of the epigenetic modifications identified in cognitive processes, histone acetylation has spurred considerable interest. ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/23324667?dopt=Abstract
Impact of Survivin Acetylation on its Biological Function | SpringerLink  Impact of Survivin Acetylation on its Biological Function | SpringerLink
David Dannheisig investigates the influence of lysine129 acetylation on the biological function of survivin including ... In his research, David Dannheisig investigates the influence of lysine129 acetylation on the biological function of survivin ... Zellbiologie Cancer Cell Biology Protein Interaction Studies Survivin Acetylation ...
more infohttps://link.springer.com/book/10.1007%2F978-3-658-18623-4
Aspirin chemically modifies human hemoglobin through acetylation.  Aspirin chemically modifies human hemoglobin through acetylation.
The rate of acetylation of hemoglobulin increased with pH up to approximately pH 8,5. Structural studies were done on ... There was no difference in the rate of acetylation of oxy- and deoxyhemoglobin. ASA acetylated column-purified hemoglobin A ... Quantitation of the extent of acetylation by densitometric scanning of gels agreed very well with estimates obtained from ...
more infohttp://www.greenmedinfo.com/article/aspirin-chemically-modifies-human-hemoglobin-through-acetylation
Acetylation | SCBT - Santa Cruz Biotechnology  Acetylation | SCBT - Santa Cruz Biotechnology
Buy Acetylation products, for use in various immunoassays including Flow Cytometry, Immunofluorescense, and ... Acetylation. Santa Cruz Biotechnology now offers a broad range of products for Acetylation research. Lysine acetylation is an ... An acid chloride reagent used for acetylation 75-36-5. sc-207253 sc-207253A 25 g. 500 g. $29.00 $65.00 0 ... Preserves the acetylation state of acetyl-lysine modified proteins sc-362323 2 ml. $55.00 1 ...
more infohttps://www.scbt.com/scbt/browse/Chemicals-Research-Reagents-by-Application-Acetylation/_/N-ai8p3o
Heart Failure Linked To Increased Acetylation Of Mitochondrial Proteins  Heart Failure Linked To Increased Acetylation Of Mitochondrial Proteins
Increased levels of acetylation of mitochondrial proteins involved in energy metabolism subsequently contribute to the ... Heart Failure Linked To Increased Acetylation Of Mitochondrial Proteins. by Shirley Johanna on February 26, 2016 at 5:44 PM ... Using an unbiased screen to look for changes in protein acetylation, the researchers profiled heart tissue from 5 end-stage ... Further, in a mouse model, they detected elevated levels of mitochondrial protein acetylation at the earliest stages of heart ...
more infohttps://www.medindia.net/news/heart-failure-linked-to-increased-acetylation-of-mitochondrial-proteins-158128-1.htm
peptidyl-lysine acetylation Antibodies | Invitrogen
                       
                       
                
		        ...  peptidyl-lysine acetylation Antibodies | Invitrogen ...
Antibodies for proteins involved in peptidyl-lysine acetylation pathways, according to their Panther/Gene Ontology ... Antibodies for proteins involved in peptidyl-lysine acetylation pathways; according to their Panther/Gene Ontology ...
more infohttps://www.thermofisher.com/antibody/primary/panther/peptidyl-lysine%20acetylation
Effects of α-tubulin acetylation on microtubule structure and stability | PNAS  Effects of α-tubulin acetylation on microtubule structure and stability | PNAS
These defects can be reversed by restoring αK40 acetylation levels (18). On the other hand, elevated levels of αK40 acetylation ... Effects of α-tubulin acetylation on microtubule structure and stability. Lisa Eshun-Wilson, Rui Zhang, Didier Portran, Maxence ... Effects of α-tubulin acetylation on microtubule structure and stability. Lisa Eshun-Wilson, Rui Zhang, Didier Portran, Maxence ... 1986) The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules. J Cell Biol 103: ...
more infohttps://www.pnas.org/content/116/21/10366.full
Frontiers | Dynamic Protein Acetylation in Plant-Pathogen Interactions | Plant Science  Frontiers | Dynamic Protein Acetylation in Plant-Pathogen Interactions | Plant Science
Protein acetylation is an emerging biochemical modification that appears to play central roles during host-pathogen ... To date, research in this area has focused on two main themes linking protein acetylation to plant immune signaling. Firstly, ... Collectively these findings suggest that the acetylation level for a range of host proteins may be modulated to alter the ... To date, research in this area has focused on two main themes linking protein acetylation to plant immune signaling. Firstly, ...
more infohttps://www.frontiersin.org/articles/10.3389/fpls.2016.00421/full
Histone H4 Total Acetylation Detection Fast Kit (Colorimetric) (ab115125)  Histone H4 Total Acetylation Detection Fast Kit (Colorimetric) (ab115125)
Histone H4 Total Acetylation Detection Fast Kit (Colorimetric) Epigenetic Kits datasheet (ab115125). Abcam offers quality ... Histone H4 Total Acetylation Detection Fast Kit (Colorimetric). See all Histone H4 acetylation kits. ... The reversible lysine acetylation of histone H4 may play a vital role in the regulation of many cellular processes including ... Acetylation of histones such histone H4 has been involved in the regulation of chromatin structure and the recruitment of ...
more infohttp://www.abcam.com/histone-h4-total-acetylation-detection-fast-kit-colorimetric-ab115125.html
Regulation of human SRY subcellular distribution by its acetylation/deacetylation.  Regulation of human SRY subcellular distribution by its acetylation/deacetylation.
... Thevenet L., Mejean C., Moniot B., Bonneaud ... We show that acetylation participates in the nuclear localisation of SRY by increasing SRY interaction with importin beta, ... In this study, we demonstrate that interaction of the human SRY with histone acetyltransferase p300 induces the acetylation of ... we suggest that acetylation and deacetylation of SRY may be important mechanisms for regulating SRY activity during mammalian ...
more infohttps://www.uniprot.org/citations/15297880
Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux | Science  Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux | Science
Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux. By Qijun Wang, Yakun Zhang, Chen ... Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux. By Qijun Wang, Yakun Zhang, Chen ... Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux Message Subject. (Your Name) has ... Lysine acetylation regulates many eukaryotic cellular processes, but its function in prokaryotes is largely unknown. We ...
more infohttp://science.sciencemag.org/content/327/5968/1004
Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation | PNAS  Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation | PNAS
... by histone acetylation of the chromatin associated with the p21WAF1 gene and that HDAC inhibitor-induced histone acetylation ... by the degree of acetylation of the gene-associated histones and that this induced increase in acetylation is gene selective. ... 2B and 5A). No change in the levels of histone H4 acetylation was detected after culture with SAHA (Fig. 5B). Taken together, ... In this study, we have examined the effects of SAHA on the acetylation of histones in the chromatin of the p21WAF1 gene. We ...
more infohttps://www.pnas.org/content/97/18/10014?ijkey=bbadc7c1e8d50640bbd58d7345d80f796fa8dcdc&keytype2=tf_ipsecsha
  • We then suggest a role for alterations in mitochondrial acetylation states during age-related conditions of heart failure and cancer, as well as review its potential role in human longevity. (hindawi.com)
  • Further, in a mouse model, they detected elevated levels of mitochondrial protein acetylation at the earliest stages of heart failure. (medindia.net)
  • Histone H4 Total Acetylation Detection Fast Kit (Colorimetric) is suitable for specifically measuring total histone H4 acetylation using a variety of mammalian cells including fresh and frozen tissues, and cultured adherent and suspension cells. (abcam.com)
  • Acetylation refers to the process of introducing an acetyl group (resulting in an acetoxy group) into a compound, namely the substitution of an acetyl group for an active hydrogen atom. (wikipedia.org)
  • Focused proteomic approaches are needed to get an overview of the extent of internal protein acetylation in archaea. (hindawi.com)
  • However, results obtained during recent years have revealed that this belief is far from being true and that-in contrast-N-terminal protein acetylation adds to the ever growing number of biological functions that combine eukaryotes and archaea to the exclusion of the bacteria. (hindawi.com)
  • However, the information about protein acetylation in archaea is still pretty limited. (hindawi.com)
  • Therefore, this paper plays a dual role on the one hand it will summarize the results about protein acetylation in archaea, and on the other hand it has the hope to nudge further research in this fascinating and mainly unexplored area. (hindawi.com)
  • This review discusses the O-acetylation status of CPSs and its role in the immunological responses of these antigens. (mdpi.com)
  • This review will focus on summarizing our current understanding of the roles of protein acetylation in plant defense and highlight the utility of proteomics approaches to uncover the complete repertoire of acetylation changes triggered by pathogen infection. (frontiersin.org)
  • Histone acetylation: molecular mnemonics on the chromatin. (nih.gov)
  • View detailed Acetylation product specifications, including CAS number, molecular weight, molecular formula and chemical structure, by clicking on the product name. (scbt.com)
  • Using high-resolution cryo-EM maps of acetylated and deacetylated microtubules, in conjunction with molecular-dynamics methods, we found that acetylation restricts the range of motion of the αK40 loop. (pnas.org)
  • Here, we demonstrate that Hsp70 preferentially facilitates protein refolding after stress, gradually switching to protein degradation via a mechanism dependent on ARD1-mediated Hsp70 acetylation. (sigmaaldrich.com)
  • Using an unbiased screen to look for changes in protein acetylation, the researchers profiled heart tissue from 5 end-stage heart failure patients who went on to receive heart transplants. (medindia.net)