Protein Methyltransferases: Enzymes that catalyze the methylation of amino acids after their incorporation into a polypeptide chain. S-Adenosyl-L-methionine acts as the methylating agent. EC 2.1.1.Methyltransferases: A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (Dorland, 28th ed) EC 2.1.1.DNA (Cytosine-5-)-Methyltransferase: An enzyme that catalyzes the transfer of a methyl group from S-ADENOSYLMETHIONINE to the 5-position of CYTOSINE residues in DNA.tRNA Methyltransferases: Enzymes that catalyze the S-adenosyl-L-methionine-dependent methylation of ribonucleotide bases within a transfer RNA molecule. EC 2.1.1.DNA-Cytosine Methylases: Methylases that are specific for CYTOSINE residues found on DNA.Histone-Lysine N-Methyltransferase: An enzyme that catalyzes the methylation of the epsilon-amino group of lysine residues in proteins to yield epsilon mono-, di-, and trimethyllysine. EC 2.1.1.43.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)S-Adenosylmethionine: Physiologic methyl radical donor involved in enzymatic transmethylation reactions and present in all living organisms. It possesses anti-inflammatory activity and has been used in treatment of chronic liver disease. (From Merck, 11th ed)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.DNA Modification Methylases: Enzymes that are part of the restriction-modification systems. They are responsible for producing a species-characteristic methylation pattern, on either adenine or cytosine residues, in a specific short base sequence in the host cell's own DNA. This methylated sequence will occur many times in the host-cell DNA and remain intact for the lifetime of the cell. Any DNA from another species which gains entry into a living cell and lacks the characteristic methylation pattern will be recognized by the restriction endonucleases of similar specificity and destroyed by cleavage. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms.DNA Methylation: Addition of methyl groups to DNA. DNA methyltransferases (DNA methylases) perform this reaction using S-ADENOSYLMETHIONINE as the methyl group donor.Betaine-Homocysteine S-Methyltransferase: A ZINC metalloenzyme that catalyzes the transfer of a methyl group from BETAINE to HOMOCYSTEINE to produce dimethylglycine and METHIONINE, respectively. This enzyme is a member of a family of ZINC-dependent METHYLTRANSFERASES that use THIOLS or selenols as methyl acceptors.Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.S-Nitrosothiols: A group of organic sulfur-containing nitrites, alkyl thionitrites. S-Nitrosothiols include compounds such as S-NITROSO-N-ACETYLPENICILLAMINE and S-NITROSOGLUTATHIONE.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Vitamin U: A vitamin found in green vegetables. It is used in the treatment of peptic ulcers, colitis, and gastritis and has an effect on secretory, acid-forming, and enzymatic functions of the intestinal tract.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.Wheat Germ Agglutinins: Lectins purified from the germinating seeds of common wheat (Triticum vulgare); these bind to certain carbohydrate moieties on cell surface glycoproteins and are used to identify certain cell populations and inhibit or promote some immunological or physiological activities. There are at least two isoforms of this lectin.O(6)-Methylguanine-DNA Methyltransferase: An enzyme that transfers methyl groups from O(6)-methylguanine, and other methylated moieties of DNA, to a cysteine residue in itself, thus repairing alkylated DNA in a single-step reaction. EC 2.1.1.63.Purine-Nucleoside Phosphorylase: An enzyme that catalyzes the reaction between a purine nucleoside and orthophosphate to form a free purine plus ribose-5-phosphate. EC 2.4.2.1.Thionucleosides: Nucleosides in which the base moiety is substituted with one or more sulfur atoms.Ubiquitin: A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.Ubiquitin-Protein Ligases: A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.Peptide Termination Factors: Proteins that are involved in the peptide chain termination reaction (PEPTIDE CHAIN TERMINATION, TRANSLATIONAL) on RIBOSOMES. They include codon-specific class-I release factors, which recognize stop signals (TERMINATOR CODON) in the MESSENGER RNA; and codon-nonspecific class-II release factors.Peptide Chain Termination, Translational: A process of GENETIC TRANSLATION whereby the terminal amino acid is added to a lengthening polypeptide. This termination process is signaled from the MESSENGER RNA, by one of three termination codons (CODON, TERMINATOR) that immediately follows the last amino acid-specifying CODON.Codon, Terminator: Any codon that signals the termination of genetic translation (TRANSLATION, GENETIC). PEPTIDE TERMINATION FACTORS bind to the stop codon and trigger the hydrolysis of the aminoacyl bond connecting the completed polypeptide to the tRNA. Terminator codons do not specify amino acids.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.Ribosome Subunits, Large, Eukaryotic: The large subunit of the 80s ribosome of eukaryotes. It is composed of the 28S RIBOSOMAL RNA, the 5.8S RIBOSOMAL RNA, the 5S RIBOSOMAL RNA, and about 50 different RIBOSOMAL PROTEINS.Cell Differentiation: Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Spermatocytes: Male germ cells derived from SPERMATOGONIA. The euploid primary spermatocytes undergo MEIOSIS and give rise to the haploid secondary spermatocytes which in turn give rise to SPERMATIDS.Ribonucleoproteins, Small Nuclear: Highly conserved nuclear RNA-protein complexes that function in RNA processing in the nucleus, including pre-mRNA splicing and pre-mRNA 3'-end processing in the nucleoplasm, and pre-rRNA processing in the nucleolus (see RIBONUCLEOPROTEINS, SMALL NUCLEOLAR).SMN Complex Proteins: A complex of proteins that assemble the SNRNP CORE PROTEINS into a core structure that surrounds a highly conserved RNA sequence found in SMALL NUCLEAR RNA. They are found localized in the GEMINI OF COILED BODIES and in the CYTOPLASM. The SMN complex is named after the Survival of Motor Neuron Complex Protein 1, which is a critical component of the complex.Golgi Apparatus: A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)Pectins: High molecular weight polysaccharides present in the cell walls of all plants. Pectins cement cell walls together. They are used as emulsifiers and stabilizers in the food industry. They have been tried for a variety of therapeutic uses including as antidiarrheals, where they are now generally considered ineffective, and in the treatment of hypercholesterolemia.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Arabidopsis Proteins: Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.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.Breast Neoplasms: Tumors or cancer of the human BREAST.Breast: In humans, one of the paired regions in the anterior portion of the THORAX. The breasts consist of the MAMMARY GLANDS, the SKIN, the MUSCLES, the ADIPOSE TISSUE, and the CONNECTIVE TISSUES.Triple Negative Breast Neoplasms: Breast neoplasms that do not express ESTROGEN RECEPTORS; PROGESTERONE RECEPTORS; and do not overexpress the NEU RECEPTOR/HER-2 PROTO-ONCOGENE PROTEIN.Receptors, Progesterone: Specific proteins found in or on cells of progesterone target tissues that specifically combine with progesterone. The cytosol progesterone-receptor complex then associates with the nucleic acids to initiate protein synthesis. There are two kinds of progesterone receptors, A and B. Both are induced by estrogen and have short half-lives.Cell Line, Tumor: A cell line derived from cultured tumor cells.Receptors, Estrogen: Cytoplasmic proteins that bind estrogens and migrate to the nucleus where they regulate DNA transcription. Evaluation of the state of estrogen receptors in breast cancer patients has become clinically important.D-Aspartate Oxidase: An FAD-dependent peroxisomal flavoenzyme, this catalyzes the oxidative deamination of D-ASPARTATE to OXALOACETATE and AMMONIA using oxygen as electron acceptor.Adenosylhomocysteinase: An enzyme which catalyzes the catabolism of S-ADENOSYLHOMOCYSTEINE to ADENOSINE and HOMOCYSTEINE. It may play a role in regulating the concentration of intracellular adenosylhomocysteine.S-Adenosylhomocysteine: 5'-S-(3-Amino-3-carboxypropyl)-5'-thioadenosine. Formed from S-adenosylmethionine after transmethylation reactions.D-Aspartic Acid: The D-isomer of ASPARTIC ACID.Protein O-Methyltransferase: An enzyme that catalyzes the transfer of methyl groups from S-adenosylmethionine to free carboxyl groups of a protein molecule forming methyl esters. EC 2.1.1.-.Arginine: An essential amino acid that is physiologically active in the L-form.Prostatic Neoplasms: Tumors or cancer of the PROSTATE.

Isoaspartate in ribosomal protein S11 of Escherichia coli. (1/608)

Isoaspartyl sites, in which an aspartic acid residue is linked to its C-flanking neighbor via its beta-carboxyl side chain, are generally assumed to be an abnormal modification arising as proteins age. The enzyme protein L-isoaspartate methyltransferase (PIMT), present in many bacteria, plants, and animals, catalyzes the conversion of isoaspartate to normal alpha-linked aspartyl bonds and is thought to serve an important repair function in cells. Having introduced a plasmid into Escherichia coli that allows high-level expression of rat PIMT, we explored the possibility that the rat enzyme reduces isoaspartate levels in E. coli proteins, a result predicted by the repair hypothesis. The present study demonstrates that this is indeed the case; E. coli cells expressing rat PIMT had significantly lower isoaspartate levels than control cells, especially in stationary phase. Moreover, the distribution of isoaspartate-containing proteins in E. coli differed dramatically between logarithmic- and stationary-phase cultures. In stationary-phase cells, a number of proteins in the molecular mass range of 66 to 14 kDa contained isoaspartate, whereas in logarithmic-phase cells, nearly all of the detectable isoaspartate resided in a single 14-kDa protein which we identified as ribosomal protein S11. The near stoichiometric levels of isoaspartate in S11, estimated at 0.5 mol of isoaspartate per mol of S11, suggests that this unusual modification may be important for S11 function.  (+info)

Cysteine carboxyl O-methylation of human placental 23 kDa protein. (2/608)

C-Terminal carboxyl methylation of a human placental 23 kDa protein catalyzed by membrane-associated methyltransferase has been investigated. The 23 kDa protein substrate methylated was partially purified by DEAE-Sephacel, hydroxyapatite and Sephadex G-100 gel filtration chromatographies. The substrate protein was eluted on Sephadex G-100 gel filtration chromatography as a protein of about 29 kDa. In the absence of Mg2+, the methylation was stimulated by guanine nucleotides (GTP, GDP and GTPgammaS), but in the presence of Mg2+, only GTPgammaS stimulated the methylation which was similar to the effect on the G25K/rhoGDI complex. AFC, an inhibitor of C-terminal carboxyl methylation, inhibited the methylation of human placental 23 kDa protein. These results suggests that the substrate is a small G protein different from the G25K and is methylated on C-terminal isoprenylated cysteine residue. This was also confirmed by vapor phase analysis. The methylated substrate protein was redistributed to membrane after in vitro methylation, suggesting that the methylation of this protein is important for the redistribution of the 23 kDa small G protein for its putative role in intracellular signaling.  (+info)

Phenotypic analysis of seizure-prone mice lacking L-isoaspartate (D-aspartate) O-methyltransferase. (3/608)

Within proteins and peptides, both L-asparaginyl and L-aspartyl residues spontaneously degrade, generating isomerized and racemized aspartyl residues. The enzyme protein L-isoaspartate (D-aspartate) O-methyltransferase (E.C. 2.1.1.77) initiates the conversion of L-isoaspartyl and D-aspartyl residues to normal L-aspartyl residues. This "repair" reaction helps to maintain proper protein conformation by preventing the accumulation of damaged proteins containing abnormal amino acid residues. Pcmt1-/- mice manifest two key phenotypes: a fatal seizure disorder and retarded growth. In this study, we characterized both phenotypes and demonstrated that they are linked. Continuous electroencephalogram monitoring of Pcmt1-/- mice revealed that abnormal cortical activity for approximately 50% of each 24-h period, even in mice that had no visible evidence of convulsions. The fatal seizure disorder in Pcmt1-/- mice can be mitigated but not eliminated by antiepileptic drugs. Interestingly, antiepileptic therapy normalized the growth of Pcmt1-/- mice, suggesting that the growth retardation is due to seizures rather than a global disturbance in growth at the cellular level. Consistent with this concept, the growth rate of Pcmt1-/- fibroblasts was indistinguishable from that of wild-type fibroblasts.  (+info)

Probing the molecular environment of membrane proteins in vivo. (4/608)

The split-Ubiquitin (split-Ub) technique was used to map the molecular environment of a membrane protein in vivo. Cub, the C-terminal half of Ub, was attached to Sec63p, and Nub, the N-terminal half of Ub, was attached to a selection of differently localized proteins of the yeast Saccharomyces cerevisiae. The efficiency of the Nub and Cub reassembly to the quasi-native Ub reflects the proximity between Sec63-Cub and the Nub-labeled proteins. By using a modified Ura3p as the reporter that is released from Cub, the local concentration between Sec63-Cub-RUra3p and the different Nub-constructs could be translated into the growth rate of yeast cells on media lacking uracil. We show that Sec63p interacts with Sec62p and Sec61p in vivo. Ssh1p is more distant to Sec63p than its close sequence homologue Sec61p. Employing Nub- and Cub-labeled versions of Ste14p, an enzyme of the protein isoprenylation pathway, we conclude that Ste14p is a membrane protein of the ER. Using Sec63p as a reference, a gradient of local concentrations of different t- and v-SNARES could be visualized in the living cell. The RUra3p reporter should further allow the selection of new binding partners of Sec63p and the selection of molecules or cellular conditions that interfere with the binding between Sec63p and one of its known partners.  (+info)

Characterization of prenylated protein methyltransferase in Leishmania. (5/608)

Prenylated protein methyltransferase, an enzyme involved in the post-translational modification of many signalling proteins, has been characterized in a parasitic flagellated protozoan, Leishmania donovani. The activity of this enzyme was monitored by the methylation of an artificial substrate, an S-prenylated cysteine analogue, with S-adenosyl-l-[methyl-(3)H]methionine as methyl donor. More than 85% of the methyltransferase activity was associated with membranes. The enzyme methylates N-acetyl-S-trans, trans-farnesyl-l-cysteine and N-acetyl-S-all-trans-geranylgeranyl-l-cysteine, but N-acetyl-S-trans, trans-geranyl-l-cysteine only very weakly. In contrast with the enzyme from mammals, the leishmanial enzyme had a greater affinity for the farnesylated substrate than for the geranylgeranylated one. Activity in vitro was not modulated by cAMP, protein kinase C activator or guanosine 5'-[gamma-thio]triphosphate. An analysis of the endogenous substrates showed that the carboxymethylated proteins were also isoprenylated. The main carboxymethylated proteins have molecular masses of 95, 68, 55, 46, 34-23, 18 and less than 14 kDa. Treatment of cells with N-acetyl-S-trans,trans-farnesyl-l-cysteine decreased the carboxymethylation level, whereas treatment with guanosine 5'-[gamma-thio]triphosphate increased the carboxymethylation of various proteins, particularly those of molecular masses 30-20 kDa.  (+info)

Isoprenylcysteine-O-carboxyl methyltransferase regulates aldosterone-sensitive Na(+) reabsorption. (6/608)

The Xenopus laevis distal tubule epithelial cell line A6 was used as a model epithelia to study the role of isoprenylcysteine-O-carboxyl methyltransferase (pcMTase) in aldosterone-mediated stimulation of Na(+) transport. Polyclonal antibodies raised against X. laevis pcMTase were immunoreactive with a 33-kDa protein in whole cell lysate. These antibodies were also reactive with a 33-kDa product from in vitro translation of the pcMTase cDNA. Aldosterone application increased pcMTase activity resulting in elevation of total protein methyl esterification in vivo, but pcMTase protein levels were not affected by steroid, suggesting that aldosterone increased activity independent of enzyme number. Inhibition of pcMTase resulted in a reduction of aldosterone-induced Na(+) transport demonstrating the necessity of pcMTase-mediated transmethylation for steroid induced Na(+) reabsorption. Transfection with an eukaryotic expression construct containing pcMTase cDNA increased pcMTase protein level and activity. This resulted in potentiation of the natriferic actions of aldosterone. However, overexpression did not change Na(+) reabsorption in the absence of steroid, suggesting that pcMTase activity is not limiting Na(+) transport in the absence of steroid, but that subsequent to aldosterone addition, pcMTase activity becomes limiting. These results suggest that a critical transmethylation is necessary for aldosterone-induction of Na(+) transport. It is likely that the protein catalyzing this methylation is isoprenylcysteine-O-carboxyl methyltransferase and that aldosterone activates pcMTase without affecting transferase expression.  (+info)

Efficient adaptational demethylation of chemoreceptors requires the same enzyme-docking site as efficient methylation. (7/608)

The mechanistic basis of sensory adaptation and gradient sensing in bacterial chemotaxis is reversible covalent modification of transmembrane chemoreceptors, methylation, and demethylation at specific glutamyl residues in their cytoplasmic domains. These reactions are catalyzed by a dedicated methyltransferase CheR and a dedicated methylesterase CheB. The esterase is also a deamidase that creates certain methyl-accepting glutamyls by hydrolysis of glutamine side chains. We investigated the action of CheB and its activated form, phospho-CheB, on a truncated form of the aspartate receptor of Escherichia coli that was missing the last 5 aa of the intact receptor. The deleted pentapeptide is conserved in several chemoreceptors in enteric and related bacteria. The truncated receptor was much less efficiently demethylated and deamidated than intact receptor, but essentially was unperturbed for kinase activation or transmembrane signaling. CheB bound specifically to an affinity column carrying the isolated pentapeptide, implying that in the intact receptor the pentapeptide serves as a docking site for the methylesterase/deamidase and that the truncated receptor was inefficiently modified because the enzyme could not dock. It is striking that the same pentapeptide serves as an activity-enhancing docking site for the methyltransferase CheR, the other enzyme involved in adaptational covalent modification of chemoreceptors. A shared docking site raises the tantalizing possibility that relative rates of methylation and demethylation could be influenced by competition between the two enzymes at that site.  (+info)

The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. (8/608)

To expand our understanding of the role of Jak2 in cellular signaling, we used the yeast two-hybrid system to identify Jak2-interacting proteins. One of the clones identified represents a human homologue of the Schizosaccaromyces pombe Shk1 kinase-binding protein 1, Skb1, and the protein encoded by the Saccharomyces cerevisiae HSL7 (histone synthetic lethal 7) gene. Since no functional motifs or biochemical activities for this protein or its homologues had been reported, we sought to determine a biochemical function for this human protein. We demonstrate that this protein is a protein methyltransferase. This protein, designated JBP1 (Jak-binding protein 1), and its homologues contain motifs conserved among protein methyltransferases. JBP1 can be cross-linked to radiolabeled S-adenosylmethionine (AdoMet) and methylates histones (H2A and H4) and myelin basic protein. Mutants containing substitutions within a conserved region likely to be involved in AdoMet binding exhibit little or no activity. We mapped the JBP1 gene to chromosome 14q11.2-21. In addition, JBP1 co-immunoprecipitates with several other proteins, which serve as methyl group acceptors and which may represent physiological targets of this methyltransferase. Messenger RNA for JBP1 is widely expressed in human tissues. We have also identified and sequenced a homologue of JBP1 in Drosophila melanogaster. This report provides a clue to the biochemical function for this conserved protein and suggests that protein methyltransferases may have a role in cellular signaling.  (+info)

A sequence variant of histone H2A called H2AX is one of the important components of chromatin involved in DNA damage response induced by different genotoxic tensions. loss in normal cells and tissues as well as in those deficient in ATM, DNA-PK, and DSB repair proteins activity. The results of the latest scientific research of the low-dose irradiation phenomenon are offered including the bystander effect and the adaptive Piboserod IC50 response estimated by H2AX detection in cells and tissues. Keywords: Phosphorylation, Histone H2AX, Dephoshorylation, DNA double-strand breaks Introduction DNA double-strand breaks (DSBs) are the most dangerous lesions induced by a variety of treatments including ionizing radiation (IR), radiomimetic drugs, and lasers action. DSB removal is usually determinated by DSB repair system efficiency and is usually crucial for cell survival. Unsuccessful DSB repair prospects to the appearance of chromosomal aberrations in mitosis and potentially could induce malignancy. ...
A sequence variant of histone H2A called H2AX is one of the important components of chromatin involved in DNA damage response induced by different genotoxic tensions. loss in normal cells and tissues as well as in those deficient in ATM, DNA-PK, and DSB repair proteins activity. The results of the latest scientific research of the low-dose irradiation phenomenon are offered including the bystander effect and the adaptive Piboserod IC50 response estimated by H2AX detection in cells and tissues. Keywords: Phosphorylation, Histone H2AX, Dephoshorylation, DNA double-strand breaks Introduction DNA double-strand breaks (DSBs) are the most dangerous lesions induced by a variety of treatments including ionizing radiation (IR), radiomimetic drugs, and lasers action. DSB removal is usually determinated by DSB repair system efficiency and is usually crucial for cell survival. Unsuccessful DSB repair prospects to the appearance of chromosomal aberrations in mitosis and potentially could induce malignancy. ...
0. by California State University, San Bernardino and considered exempt due to nonhuman subject research status. 3. Results Table 1 demonstrates the distribution of sociodemographic characteristics among Hispanic adults categorized by users and nonusers of substances in lifetime, past year, Procyanidin B1 IC50 and past month, with significant differences noted between the two groups (< 0.05). Females were less likely to report lifetime material use (35%) as compared to males (50%) as did those living in poverty (less than 100% FPL = 34%, 100C199% = 39%, and 200% or more = 50%). A higher percent of those who were interviewed in English (54%) reported lifetime material use compared to those interviewed in Spanish (18%). Similarly, among those with influence of religious beliefs in life, approximately 39% reported lifetime material use compared to significantly higher proportion (53%) among those with lower or no religious influence in life. Among those with history of incarceration, a ...
Hypertrophy can be an adaptive response that allows organs to meet up increased functional needs appropriately. missing a catalytic subunit of Cn (CnA?/? or CnA?/?), we discovered that high blood sugar activates CnA selectively, whereas CnA is dynamic constitutively. Furthermore, CnA however, not CnA mediates hypertrophy. Next, we discovered that chronic reactive air species era in response to high blood sugar is normally attenuated in CnA?/? cells, recommending that Cn is normally of Nox upstream. In keeping with this, lack of CnA reduces basal blocks and appearance great blood sugar induction of Nox2 and Nox4. Inhibition of nuclear aspect of turned on T cells (NFAT), a CnA-regulated transcription aspect, reduces Nox2 and Nox4 appearance, whereas NFAT overexpression boosts Nox4 and Nox2, indicating that the CnA/NFAT pathway modulates Nox. These data reveal which the CnA/NFAT pathway regulates Nox and has an important function in high glucose-mediated hypertrophic replies in the kidney. ...
... , Isoprenylcysteine carboxylmethyltransferase (Icmt) catalyzes the last of the three-step posttranslational protein prenylation process for the so-called CaaX proteins, which includes many signaling ...
Pancreatic pathology of representative 4-month-old mice of the indicated genotypes. Top panels show the gross specimen; asterisks indicate the pancreas in situ and rulers show centimeter marks. Middle panels: The ICMT-deficient pancreas to the right is larger, with fibrotic nodules and a cyst (arrow). Lower panels show H&E-stained sections from the same pancreata. Both normal ducts (arrowhead) and PanINs (arrow) are visible in the ...
A major interest of Professor Steven Clarkes Laboratory is understanding the biochemistry of the aging process. The group is particularly interested in the generation of age-damaged proteins by spontaneous chemical reactions and the physiological role of cellular enzymes that can reverse at least some portion of the damage. They have focused their efforts on the degradation of aspartic acid and asparagine residues and the subsequent metabolism of their racemized and isomerized derivatives. The group is presently determining the biological role of protein methyltransferases that can initiate the conversion of D-aspartyl residues to the L-configuration as well as the conversion of isopeptide linkages to normal peptide bonds. Such "repair" reactions may greatly increase the useful lifetime of cellular proteins and may help insure organismal survival. View Professor Clarkes YouTube Lecture ...
Protein methyltransferases (PMTs) and demethylases (PDMTs) are a class of approximately 100 enzymes that modify histone and non-histone proteins and were recently reported to be mutated, amplified and overexpressed in a significant proportion of cancers, including squamous cell carcinoma of the head and neck (SCCHN).. Dr. Salouras laboratory aims to elucidate the role of protein methylation mediated by PMTs and PDMTs in oncogenesis, therapy resistance and immunogenicity in squamous cell carcinoma of the aerodigestive tract, with a special focus in SCCHN. Our goal is to develop a translational research program focusing on histone and non-histone protein methylation, and to introduce novel targeted PMT and PDMT inhibitors in clinical trials for head and neck cancer patients with relevant driver molecular phenotypes.. To achieve these goals, research efforts concentrate on two main inter-related projects:. Project 1: Elucidation of the oncogenic function of specific PMTs/PDMTs in SCCHN. We plan to ...
Acts as an activator of both rRNA/tRNA and protein methyltransferases (PubMed:25851604). Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA (PubMed:25851604). The heterodimer with HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on Gln-185, using S-adenosyl L-methionine as methyl donor (PubMed:18539146). The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species (PubMed:20308323). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production (PubMed:25851604).
The overarching goal of Wan laboratory is to define the molecular mechanisms of breast tumor initiation, progression, and metastasis, and to identify novel targets for therapeutic development. Particularly, the laboratory seeks to address how defects in the ubiquitin-proteasome system and other posttranslational modifiers such as protein methyltransferase and poly (ADP-ribose) polymerase would result in genomic instability, abnormal cell cycle, and aberrant signaling that predispose otherwise no...[Read full text]The overarching goal of Wan laboratory is to define the molecular mechanisms of breast tumor initiation, progression, and metastasis, and to identify novel targets for therapeutic development. Particularly, the laboratory seeks to address how defects in the ubiquitin-proteasome system and other posttranslational modifiers such as protein methyltransferase and poly (ADP-ribose) polymerase would result in genomic instability, abnormal cell cycle, and aberrant signaling that predispose ...
Kit Component:- KN200039G1, HEMK1 gRNA vector 1 in pCas-Guide vector- KN200039G2, HEMK1 gRNA vector 2 in pCas-Guide vector- KN200039D, donor vector…
Wiz Khalifa Young, Wild & Free lyrics (ft. Snoop Dogg) & video : So what we get drunk. So what we smoke weed. Were just having fun. We dont care who sees. So what we go out. ...
Rihanna, Snoop Dogg and Busta Rhymes are among the musicians who have taken to Twitter.com to congratulate Wiz Khalifa and his fiancee Amber Rose on the arrival of their first child.The model gave birth to the couples son, Sebastian Taylor...
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Search for mouse SNPs represented in dbSNP by gene or genome region. Results include selected strains. Filter by dbSNP function class.
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The attract package contains the following man pages: AttractorModuleSet-class attract-package buildCorMatrix buildCustomIncidenceMatrix buildKeggIncidenceMatrix calcFuncSynexprs calcInform calcModfstat calcRss exprs.dat filterDataSet findAttractors findCorrPartners findOnepwaySynexprs findSynexprs flagPwayExists getCustomGenes getPwayGenes loring.eset plotsynexprs removeFlatGenes samp.info subset.loring.eset SynExpressionSet-class
Shop Leucine carboxyl methyltransferase ELISA Kit, Recombinant Protein and Leucine carboxyl methyltransferase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Farnesylcysteine lyase (EC 1.8.3.6, FC lyase, FCLY) is an enzyme with systematic name S-(2E,6E)-farnesyl-L-cysteine oxidase. This enzyme catalyses the following chemical reaction S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O ⇌ {\displaystyle \rightleftharpoons } (2E,6E)-farnesal + L-cysteine + H2O2 Farnesylcysteine lyase is a flavoprotein (FAD). Huizinga, D.H.; Denton, R.; Koehler, K.G.; Tomasello, A.; Wood, L.; Sen, S.E.; Crowell, D.N. (2010). "Farnesylcysteine lyase is involved in negative regulation of abscisic acid signaling in Arabidopsis". Mol Plant. 3 (1): 143-155. doi:10.1093/mp/ssp091. PMC 2807925 . PMID 19969520. Crowell, D.N.; Huizinga, D.H.; Deem, A.K.; Trobaugh, C.; Denton, R.; Sen, S.E. (2007). "Arabidopsis thaliana plants possess a specific farnesylcysteine lyase that is involved in detoxification and recycling of farnesylcysteine". Plant J. 50 (5): 839-847. doi:10.1111/j.1365-313X.2007.03091.x. PMID 17425716. Farnesylcysteine lyase at the US National Library of Medicine Medical ...
EHMT2-AS1 (ENST00000434689.2) at chr6:31883761-31884204 - EHMT2 and SLC44A4 antisense RNA 1 (from HGNC EHMT2-AS1) EHMT2 (ENST00000375537.8) at chr6:31879759-31897684 - Homo sapiens euchromatic histone lysine methyltransferase 2 (EHMT2), transcript variant 2, mRNA. (from RefSeq NM_006709) EHMT2 (ENST00000421926.6) at chr6_GL000250v2_alt:3212374-3230306 - Homo sapiens euchromatic histone lysine methyltransferase 2 (EHMT2), transcript variant 2, mRNA. (from RefSeq NM_006709) EHMT2 (ENST00000450075.6) at chr6_GL000251v2_alt:3357184-3375109 - Homo sapiens euchromatic histone lysine methyltransferase 2 (EHMT2), transcript variant 2, mRNA. (from RefSeq NM_006709) EHMT2 (ENST00000429506.6) at chr6_GL000252v2_alt:3127533-3145458 - Homo sapiens euchromatic histone lysine methyltransferase 2 (EHMT2), transcript variant 2, mRNA. (from RefSeq NM_006709) EHMT2 (ENST00000420336.6) at chr6_GL000254v2_alt:3221824-3239756 - Homo sapiens euchromatic histone lysine methyltransferase 2 (EHMT2), transcript variant 2, ...
Histone Methyltransferase Activity/Inhibition Assay Kit (H3-K27) is use for measuring HMT activity/inhibition. (KA0572) - Products - Abnova
Histone methyltransferase that specifically mono- and dimethylates Lys-9 of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of Lys-56 of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates Lys-27 of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of Lys-373 of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself ...
Histone methyltransferase inhibitors used for various assays, some have entered clinical trials, which would be new cancer therapies.
This abstract related to Pulmonary Hypertension (PH) was presented at the Pulmonary Vascular Institute (PVRI) 14th Annual World Congress in Lima, Peru, in 2020.
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Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
EML741 is a histone lysine methyltransferase G9a/GLP inhibitor, with an IC50 of 23 nM, Kd of 1.13 μM for G9a. EML741 also inhibits DNMT1 (IC50, 3.1 μM), with no effect on DNMT3a or DNMT3b. EML741 exhibits low cell toxicity, and is membrane permeable and blood-brain barrier penetrated. - Mechanism of Action & Protocol.
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The unfolded protein response (UPR) is an evolutionarily conserved mechanism whereby cells respond to stress conditions that target the endoplasmic reticulum (ER). One of the major targets of the UPR is the 78kDa Glucose Regulated Protein Grp78 (BiP). The transcriptional activation of the promoter of GRP78 has been used extensively as an indicator of the onset of the UPR. The transcriptional activation of Grp78 in response to ER stress has been well documented. It is characterized by multiple transcription factors such as YY1, TFII-I, ATF6(N), and NF-Y binding to conserved promoter sequences at the onset of ER stress.; There are also epigenetic changes that occur during the activation of the Grp78 promoter. We have observed ER-stress induced binding of the histone acetyltransferase p300 to the Grp78 promoter and histone H4 acetylation. We have also seen the arginine methyltransferase PRMT1, and evidence of its action through methylation of the arginine 3 residue on histone H4. We show the ...
The unfolded protein response (UPR) is an evolutionarily conserved mechanism whereby cells respond to stress conditions that target the endoplasmic reticulum (ER). One of the major targets of the UPR is the 78kDa Glucose Regulated Protein Grp78 (BiP). The transcriptional activation of the promoter of GRP78 has been used extensively as an indicator of the onset of the UPR. The transcriptional activation of Grp78 in response to ER stress has been well documented. It is characterized by multiple transcription factors such as YY1, TFII-I, ATF6(N), and NF-Y binding to conserved promoter sequences at the onset of ER stress.; There are also epigenetic changes that occur during the activation of the Grp78 promoter. We have observed ER-stress induced binding of the histone acetyltransferase p300 to the Grp78 promoter and histone H4 acetylation. We have also seen the arginine methyltransferase PRMT1, and evidence of its action through methylation of the arginine 3 residue on histone H4. We show the ...
The SET domain is a 130 to 140 amino acid, evolutionary well conserved sequence motif that was initially characterised in the Drosophila proteins Su(var)3-9, Enhancer-of-zeste and Trithorax. In addition to these chromosomal proteins modulating gene activities and/or chromatin structure, the SET domain is found in proteins of diverse functions ranging from yeast to mammals, but also including some bacteria and viruses [(PUBMED:9487389), (PUBMED:10949293)].. The SET domains of mammalian SUV39H1 and 2 and fission yeast clr4 have been shown to be necessary for the methylation of lysine-9 in the histone H3 N terminus [(PUBMED:10949293)]. However, this histone methyltransferase (HMTase) activity is probably restricted to a subset of SET domain proteins as it requires the combination of the SET domain with the adjacent cysteine-rich regions, one located N-terminally (pre-SET) and the other posterior to the SET domain (post-SET). Post- and pre- SET regions seem then to play a crucial role when it comes ...
ATF7IP [ENSP00000440440]. Activating transcription factor 7-interacting protein 1; Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1. Required to stimulate histone methyltransferase activity of SETDB1 and facilitate the conversion of dimethylated to trimethylated H3 Lys-9 (H3K9me3). The complex formed with MBD1 and SETDB1 represses transcription and couples DNA methylation and histone H3 Lys-9 trimethylation (H3K9me3). Facilitates telomerase TERT and TERC gene expression by SP1 in cancer cells; Belongs to the MCAF family.. Synonyms: ATF7IP, ATF7IPp, hATF7IP, A0A024RAY1, A8MV73 .... Linkouts: STRING Pharos UniProt ...
Complete information for DPY30 gene (Protein Coding), Dpy-30 Histone Methyltransferase Complex Regulatory Subunit, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for LCMT1 gene (Protein Coding), Leucine Carboxyl Methyltransferase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
sp:ASH1L_MOUSE] Ash1l, 8030453L17Rik, Ash1, E430018P19Rik, Kmt2h; ASH1 like histone lysine methyltransferase; K06101 histone-lysine N-methyltransferase ASH1L [EC:2.1.1.43] ...
sp:ASH1L_MOUSE] Ash1l, 8030453L17Rik, Ash1, E430018P19Rik, Kmt2h; ASH1 like histone lysine methyltransferase; K06101 histone-lysine N-methyltransferase ASH1L [EC:2.1.1.43] ...
Background SUV39H1 is a human homologue of the dominant Drosophila PEV modifier Su(var)3ndash;9 and is composed of 412 amino acid residues. SUV39H1, as a histone methyltransferase, selectively methylates histone H3 on lysine...
Rabbit polyclonal antibody raised against synthetic peptide of SETDB2. A synthetic peptide corresponding to N-terminus of human SETDB2. (PAB5573) - Products - Abnova
Expression of WIZ (ZNF803) in cancer tissue. The cancer tissue page shows antibody staining of the protein in 20 different cancers.
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PLSCR3 (phospholipid scramblase 3 Scr3) is one of the superfamily of membrane-associated transcription regulators named Tubby-like protein (TULPs). medium LAQ824 by means of extracellular microvesicles (exosomes). Alternatively Scr3 expression didnt decrease as well as the secretion of Scr3 significantly?in 3T3 Swiss-albino fibroblasts (a parental cell-line of 3T3-L1) had not been increased by differentiation treatment. Overexpression of human being Scr3 during 3T3-L1 differentiation suppressed triacylglycerol build up and inhibited induction from the mRNAs lately stage pro-adipogenic transcription elements [CCAAT/enhancer-binding proteins α (C/EBPα) and peroxisome proliferator-activated receptor γ (PPARγ)] and X-box-binding proteins 1 (XBP1). Manifestation of early stage pro-adipogenic transcription elements (C/EBPβ and C/EBPδ) had not been considerably affected. These outcomes claim that Scr3 features as a poor regulator of adipogenesis in 3T3-L1 cells at a particular differentiation ...
During the last 2 decades genome-wide research have revealed that only a part of the human genome encodes protein; longer noncoding RNAs (lncRNAs) take into account 98% of the full total genome. GC. Right here we review the existing understanding of the natural functions and scientific areas of lncRNAs in GC. knockdown decreased YBX1 proteins level by accelerating its degradation resulting in the downregulation of p21 and development through the G1 stage from the cell routine. YBX1 plays a crucial function in the GAS5-mediated legislation from the GAS5/YBX1/p21 pathway which regulates the cell routine and modulates GC cell proliferation.60 Tumor suppressor candidate 7 Tumor suppressor candidate (TUSC)7 is downregulated in GC when compared with NAT and inhibits cell development in vitro and in vivo. TUSC7 is normally turned on by p53 through p53-reactive components in its promoter. Furthermore a repressive connections between TUSC7 and miR-23b continues to be reported mutually. The activation of ...
PROTEIN ARGININE METHYLTRANSFERASE 6 (PRMT6); FUNCTIONS IN: methyltransferase activity; INVOLVED IN: metabolic process; EXPRESSED IN: 19 plant structures; EXPRESSED DURING: 7 growth stages; CONTAINS InterPro DOMAIN/s: Methyltransferase type 11 (InterPro:IPR013216); BEST Arabidopsis thaliana protein match is: PRMT1A (PROTEIN ARGININE METHYLTRANSFERASE 1A); protein-arginine N-methyltransferase (TAIR:AT2G19670.1); Has 3635 Blast hits to 3579 proteins in 972 species: Archae - 81; Bacteria - 1747; Metazoa - 1005; Fungi - 174; Plants - 198; Viruses - 0; Other Eukaryotes - 430 (source: NCBI BLink ...
Translocation of the MLL1 gene, which encodes for the histone methyltransferase, MLL1, is found in approximately 10% of all cases of acute leukemia and is generally associated with poor patient outcomes. Recent research has pointed to an essential function for the wild-type copy of MLL1 in these leukemias. In these cells, abnormal upregulation of MLL1-directed histone methylation and subsequent overexpression of MLL1 gene targets is an essential step in the development and progression of leukemia. Efficient MLL1-catalyzed histone methylation can only be achieved when MLL1 associates with the complex of WDR5, RbBP5 and Ash2L. MLL1 complex assembly is nucleated by a highly conserved interaction between the MLL1 SET domain and WDR5. We hypothesize that blocking histone methyltransferase activity of wild-type MLL1 through inhibition of the essential WDR5-MLL1 interaction will prevent abnormal gene upregulation and transformation in leukemias with MLL1 rearrangement. Using rational design, we have ...
5507 AS1411 (formerly AGRO100) is a guanosine-rich phosphodiester oligodeoxynucleotide that is currently being tested in a Phase I clinical trial for the treatment of advanced cancer. This agent has a novel mechanism of action that involves binding to nucleolin, a multifunctional protein that is expressed abnormally by cancer cells. Binding of AS1411 to nucleolin is thought to alter the molecular interactions of nucleolin, which modulates nucleolin function and leads to antiproliferative effects. The purpose of this study was to identify nucleolin-binding proteins whose interactions with nucleolin are perturbed in AS1411-treated cancer cells. The nucleolin complex was isolated by immunoprecipitation (IP) from human prostate cancer DU145 cells. Several nucleolin-interacting proteins, including protein arginine methyltransferase 5 (PRMT5), were identified by MALDI-TOF-mass spectrometry. PRMT5 is a Type II arginine methyltransferase (makes symmetrical dimethylarginine modifications) that has been ...
Mechanistic and chiroptical studies on the desulfurization of epidithiodioxopiperazines reveal universal retention of configuration at the bridgehead carbon atoms." Cherblanc, F. L.; Lo, Y. -P.; Herrebout, W.; Bultinck, P.; Rzepa, H. S.*; Fuchter, M. J.* J. Org. Chem. 2013, 78, 11646. DOI. "On the histone lysine methyltransferase activity of fungal metabolite chaetocin" Cherblanc, F. L.; Chapman, K.; Reid, J.; Borg, A.; Sundriyal, S.; Alcazar-Fuoli, L.; Bignell, E.; Demetriades, M.; Schofield, C. J.; Dimaggio, P.; Brown, R.; Fuchter, M. J.*J. Med. Chem. 2013, 56, 8616. DOI. "Development of a cyclin-dependent kinase inhibitor devoid of ABC transporter-dependent drug resistance." Kaliszczak, M.; Patel, H.; Kroll, S. H.; Carroll, L.; Smith, G.; Delaney, S.; Heathcote, D. A.; Bondke, A.; Fuchter, M. J.; Coombes, R. C.; Barrett, A. G. M.; Ali, S.; Aboagye, E. O.* Br. J. Cancer 2013, 109, 2356. DOI. "ortho-Substituted 1,8-Diarylnaphthalenes: Conformational Thermodynamics and Kinetics" Judge, D.; ...
5-MTHF: 5-methyltetrahydrofolate; 5,10-methyltetrahydrofolate; BAX: Bcl-2-associated X protein; BHMT: betaine-homocysteine S- ... methyltransferase; CBS: cystathionine beta synthase; CGL: cystathionine gamma-lyase; DHF: dihydrofolate (vitamin B9); DMG: ...
3.67 nM/mg protein/30 mins (high affinity), and Km = 143 μM; Vmax = 7.87 nM/mg protein/30 mins (low affinity). The LD50 of N- ... In animal tissue, N-methylphenylethanolamine is formed by the action of the enzyme phenylethanolamine N-methyl transferase ( ... J.Axelrod (1962). "Purification and properties of phenylethanolamine-N-methyl transferase." J. Biol. Chem. 237 1657-1660. S. ...
Clarke, Steven G.; Tamanoi, Fuyuhiko (2006). Protein methyltransferases. Academic Press. pp. 162-172. ISBN 978-0-12-122725-8. ... In structural biology, ternary complex can also be used to describe a crystal containing a protein with two small molecules ... A ternary complex is a protein complex containing three different molecules that are bound together. ... bound, for example cofactor and substrate; or a complex formed between two proteins and a single substrate. In Immunology, ...
PRMT6: Protein arginine methyltransferase 6. *PSRC1: Proline/serine-rich coiled-coil protein 1 ... ARID4B: encoding protein AT-rich interactive domain-containing protein 4B. *ARV1 encoding protein ARV1 homolog (S. cerevisiae) ... OTUD7B: OTU domain-containing protein 7B. *PACERR encoding protein PTGS2 antisense NFKB1 complex-mediated expression regulator ... C1orf103: encoding protein Ligand-dependent nuclear receptor-interacting factor 1 (LRIF1). *C1orf109: chromosome 1 open reading ...
DNA methyltransferase • Sister-chromatid cohesion factors • Protein kinases • Cell-cycle regulators • Apoptotic factors for ... The protein encoded by this gene is found in the nucleus and is a cofactor of DNA polymerase delta. The encoded protein acts as ... Proteins binding to PCNA via the PIP-box are mainly involved in DNA replication whereas proteins binding to PCNA via APIM are ... binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein". J. ...
Cook RJ, Wagner C (1984). "Glycine N-methyltransferase is a folate binding protein of rat liver cytosol". Proceedings of the ... In addition to the methyltransferase activity, the 4S polycyclic aromatic hydrocarbon (PAH)-binding protein and GNMT are one ... Yeo EJ, Wagner C (1994). "Tissue distribution of glycine N-methyltransferase, a major folate-binding protein of liver". ... Proteins. 57 (2): 331-7. doi:10.1002/prot.20209. PMID 15340920. Luka Z, Mudd SH, Wagner C (2009). "Glycine N-methyltransferase ...
"Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase ... "Regulation of transcription by a protein methyltransferase". Science. 284 (5423): 2174-7. doi:10.1126/science.284.5423.2174. ... The nuclear receptor coactivator 2 also known as NCoA-2 is a protein that in humans is encoded by the NCOA2 gene. NCoA-2 is ... Naltner A, Ghaffari M, Whitsett JA, Yan C (2000). "Retinoic acid stimulation of the human surfactant protein B promoter is ...
"Regulation of transcription by a protein methyltransferase". Science. 284 (5423): 2174-2177. doi:10.1126/science.284.5423.2174 ... The yeast two-hybrid protein-protein interaction assay led to the identification of an array of receptor-interacting factors in ... Coactivators exist in large, modular complexes in the cell, and are known to participate in many different protein-protein ... Lee, J. W.; Choi, H. S.; Gyuris, J.; Brent, R. & Moore, D. D. (1995). "Two classes of proteins dependent on either the presence ...
... (coactivator-associated arginine methyltransferase 1), also known as PRMT4 (protein arginine N-methyltransferase 4), is ... histone-arginine N-methyltransferase coactivator-associated arginine methyltransferase 1 at the US National Library of Medicine ... "Regulation of transcription by a protein methyltransferase". Science. 284 (5423): 2174-7. doi:10.1126/science.284.5423.2174. ... "RCSB Protein Data Bank - Sequence / Structure Details for 2Y1W - CRYSTAL STRUCTURE OF COACTIVATOR ASSOCIATED ARGININE ...
The viruses encode a protein, normally a replicase, with a methyltransferase activity to allow this. Some viruses are cap- ... In this process the first protein encoded on the genome, and this the first to be translated, is a replicase. This protein will ... In non-persistent and semi-persistent viruses, these domains are in the coat protein and another protein known as the helper ... Viruses use the plant ribosomes to produce the 4-10 proteins encoded by their genome. However, since many of the proteins are ...
"Identification of proteins interacting with protein arginine methyltransferase 8: The Ewing sarcoma (EWS) protein binds ... Protein arginine methyltransferase 8 is a protein that in humans is encoded by the PRMT8 gene. Arginine methylation is a ... "Protein arginine methyltransferase 8". Retrieved 2011-12-04. Kim, J. D.; Kako, K.; Kakiuchi, M.; Park, G. G.; Fukamizu, A. ( ... Sayegh, J.; Webb, K.; Cheng, D.; Bedford, M. T.; Clarke, S. G. (2007). "Regulation of Protein Arginine Methyltransferase 8 ( ...
Protein arginine methyltransferase 7 is a protein that in humans is encoded by the PRMT7 gene. Arginine methylation is an ... "Protein arginine methyltransferase 7". Retrieved 2011-12-06. Miranda, T. B.; Miranda, M.; Frankel, A.; Clarke, S. (2004). " ... Jelinic, P.; Stehle, J. C.; Shaw, P. (2006). "The Testis-Specific Factor CTCFL Cooperates with the Protein Methyltransferase ... a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine". Journal of Biological Chemistry. 280 (5 ...
The UBQLN2 gene encodes the protein ubiquilin 2 which is responsible for controlling the degradation of ubiquitinated proteins ... Goll MG, Bestor TH (2005). "Eukaryotic cytosine methyltransferases". Annual Review of Biochemistry. 74: 481-514. doi:10.1146/ ... As that gene's name suggests, BACE1 is an enzymatic protein that cleaves the Amyloid Precursor Protein into the insoluble ... Mutations in UBQLN2 interfere with protein degradation resulting in neurodegeneration through abnormal protein aggregation.[52] ...
PDB code: Code used to identify the structure of a protein in the PDB database of protein structures. The 3D atomic structure ... Kessler C, Manta V (August 1990). "Specificity of restriction endonucleases and DNA modification methyltransferases a review ( ... Anfinsen C.B. (1973). "Principles that Govern the Folding of Protein Chains". Science. 181 (4096): 223-30. doi:10.1126/science. ... of a protein provides highly valuable information to understand the intimate details of its mechanism of action[3][4]. ...
Lysine methyltransferase 2E is a protein that in humans is encoded by the KMT2E gene. This gene is a member of the myeloid/ ... Overexpression of the protein inhibits cell cycle progression. Alternate transcriptional splice variants have been ... Lysine methyltransferase 2E". Retrieved 2016-06-02. Emerling BM, Bonifas J, Kratz CP, Donovan S, Taylor BR, Green ED, Le Beau ... lymphoid or mixed-lineage leukemia (MLL) family and encodes a protein with an N-terminal PHD zinc finger and a central SET ...
Qi C, Chang J, Zhu Y, Yeldandi AV, Rao SM, Zhu YJ (August 2002). "Identification of protein arginine methyltransferase 2 as a ... Scavenger receptor class B type 1 (SRB1) also known as SR-BI is a protein that in humans is encoded by the SCARB1 gene.[5] SR- ... Click on genes, proteins and metabolites below to link to respective articles. [§ 1] ... protein binding. • high-density lipoprotein particle binding. • lipopolysaccharide receptor activity. • amyloid-beta binding. • ...
... methyltransferases. The radical SAM methyltransferases are believed to β-methylate amino acid residues within the precursor ... Ribosomal peptide synthesis, which is the same machinery that produces all proteins found in the cell, is limited to the 20 ... Radical SAM methyltransferases are likely to methylate substrates by an unusual mechanism. Biosynthetically, β-methylations of ... Bioinformatics suggest that btmB, is an O-methyltransferase, while the other three, btmC, G and K, are radical S-adenosyl ...
N6-adenosine-methyltransferase 70 kDa subunit (METTL3) is an enzyme that in humans is encoded by the METTL3 gene. This gene ... 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. ... Leach RA, Tuck MT (2001). "Expression of the mRNA (N6-adenosine)-methyltransferase S-adenosyl-L-methionine binding subunit mRNA ... 1998). "Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase". RNA. 3 ...
Dillon SC, Zhang X, Trievel RC, Cheng X (2005). "The SET-domain protein superfamily: protein lysine methyltransferases" (PDF). ... SET domain proteins differ from other SAM-dependent methyltransferases in that they bind their substrate and SAM cofactor on ... In particular, WD40-repeat protein embryonic ectoderm development (EED) and zinc finger protein suppressor of zeste 12 (SUZ12) ... which is a product-based inhibitor of all protein methyltransferases, leading to increased cellular concentrations of SAH which ...
Protein-S-isoprenylcysteine O-methyltransferase is an enzyme that in humans is encoded by the ICMT gene. This gene encodes the ... Desrosiers RR, Nguyen QT, Beliveau R (Sep 1999). "The carboxyl methyltransferase modifying G proteins is a metalloenzyme". ... 1999). "Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi". Cell. 98 (1): 69-80. doi:10.1016 ... 2004). "Isoprenylcysteine carboxyl methyltransferase activity modulates endothelial cell apoptosis". Mol. Biol. Cell. 14 (3): ...
Methyltransferase like 16 is a protein that in humans is encoded by the METTL16 gene. GRCh38: Ensembl release 89: ... Methyltransferase like 16". Retrieved 2018-01-25. Docherty SJ, Kovas Y, Petrill SA, Plomin R (2010). "Generalist genes analysis ...
Tang J, Kao PN, Herschman HR (2000). "Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase ... "Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is ... Wada K, Inoue K, Hagiwara M (August 2002). "Identification of methylated proteins by protein arginine N-methyltransferase 1, ... The HRMT1L2 gene encodes a protein arginine methyltransferase that functions as a histone methyltransferase specific for ...
Protein arginine N-methyltransferase 2 is an enzyme that in humans is encoded by the PRMT2 gene. PRMT2 has been shown to ... "Entrez Gene: PRMT2 protein arginine methyltransferase 2". Qi, Chao; Chang Jeffrey; Zhu Yiwei; Yeldandi Anjana V; Rao Sambasiva ... 2002). "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha". J. Biol. Chem. ... 2006). "Protein Methyltransferase 2 Inhibits NF-κB Function and Promotes Apoptosis". Mol. Cell. Biol. 26 (10): 3864-74. doi: ...
Protein arginine N-methyltransferase 6 is an enzyme that in humans is encoded by the PRMT6 gene. Protein arginine N- ... "Entrez Gene: PRMT6 protein arginine methyltransferase 6". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to ... "The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity". J Biol ... 2007). "Protein methylation is required to maintain optimal HIV-1 infectivity". Retrovirology. 3: 92. doi:10.1186/1742-4690-3- ...
... binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3". J. Biol. Chem. 274 (19): ... Protein arginine N-methyltransferase 3 is an enzyme that in humans is encoded by the PRMT3 gene. Model organisms have been used ... "Entrez Gene: PRMT3 protein arginine methyltransferase 3". "Body weight data for Prmt3". Wellcome Trust Sanger Institute. " ... 2004). "DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to ...
... also activates or inhibits the activities of a number of proteins.[22] For example, quercetin is a non-specific ... The meta-hydroxyl group of catechol is methylated by catechol-O-methyltransferase. Four of the five hydroxyl groups of ... quercetin has also been found to act as an agonist of the G protein-coupled estrogen receptor (GPER).[26][27] ... "The G protein-coupled receptor GPR30 mediates c-fos up-regulation by 17beta-estradiol and phytoestrogens in breast cancer cells ...
... a type II protein arginine methyltransferase, and increased its multiprotein complex and methyltransferase activity. Activated ...
... arginines in proteins. We investigated the expressions of PRMT1 and PRMT5 in relation to their catalytic activities in rat ... Protein-arginine methylation is a posttranslational modification which yields monomethyl and dimethyl (asymmetric or symmetric ... Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver Biochim ... In fetal rat liver, the amount of expressed 42 kDa PRMT1 protein and the enzyme activity to methylate hnRNPA1 protein were 2- ...
Background During mammalian protein will not have ENGase activity and phrase. *Compelled expression of lineage-specific ... Background It is reported the iron-responsive element-binding protein 2 (IREB2) gene. by Ross Marshall ... 21] also found increased IREB2 protein in human being lung cells via assessment of COPD individuals with controls. Therefore ... Background It is reported the iron-responsive element-binding protein 2 (IREB2) gene rs2568494 polymorphism might be associated ...
We have previously reported a positive correlation between the expression of BHMT (betaine-homocysteine S-methyltransferase) ... microsomal triacylglycerol transfer protein; NASH, non-alcoholic steatohepatitis; NEFA, non-esterified fatty acid; SAM, S- ... betaine-homocysteine S-methyltransferase; CMV, cytomegalovirus; DMEM, Dulbeccos modified Eagles medium; DRB, 5,6- ... adenosylmethionine; SREBP, sterol-regulatory-element-binding protein; VLDL, very-low-density lipoprotein ...
Effects on proteins related to cellular maintenance and stress were observed in both genders. Regulated proteins were gender- ... Betaine homocysteine methyltransferase (BHMT) was induced in both genders. In addition a female-specific downregulation of ... ironhomeostatic proteins (iron-regulatory protein 1 and transferrin) were observed. Our proteomic approach revealed novel ...
SAM-dependent DNA methyltransferase [Pseudomonas oryzihabitans]. NCBI Reference Sequence: WP_044341597.1. Identical Proteins ... SAM-dependent DNA methyltransferase [Pseudomonas oryzihabitans] SAM-dependent DNA methyltransferase [Pseudomonas oryzihabitans] ... The tool works with standard single letter nucleotide or protein codes including ambiguities and can match Prosite patterns in ... The tool works with standard single letter nucleotide or protein codes including ambiguities and can match Prosite patterns in ...
RNA methyltransferase [Leptospira interrogans] RNA methyltransferase [Leptospira interrogans]. gi,446103206,ref,WP_000181061.1, ... The tool works with standard single letter nucleotide or protein codes including ambiguities and can match Prosite patterns in ... The tool works with standard single letter nucleotide or protein codes including ambiguities and can match Prosite patterns in ... This record is a non-redundant protein sequence. Please read more here. ...
We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their ... InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... Protein-lysine N-methyltransferase Efm5/EEF1AKMT1 (IPR019369). Short name: Efm5/EEF1AKMT1 Overlapping homologous superfamilies ... A new type of protein lysine methyltransferase trimethylates Lys-79 of elongation factor 1A.. Biochem. Biophys. Res. Commun. ...
We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their ... InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... Methylated-DNA-[protein]-cysteine S-methyltransferase, active site (IPR001497). Short name: MethylDNA_cys_MeTrfase_AS ... DNA-[protein]-cysteine S-methyltransferases are widely distributed and are found in various prokaryotic and eukaryotic sources ...
Protein arginine methyltransferases (PRMTs), an emerging target class in drug discovery, can methylate histones and other ... Structural biology and chemistry of protein arginine methyltransferases M. Schapira and R. Ferreira de Freitas, Med. Chem. ... Protein arginine methyltransferases (PRMTs), an emerging target class in drug discovery, can methylate histones and other ... we review the growing body of structural information characterizing this protein family, including structures in complex with ...
Protein lysine methyltransferases (PKMTs) catalyze the methylation of protein substrates, and their dysregulation has been ... 2005) The SET-domain protein superfamily: Protein lysine methyltransferases. Genome Biol 6(8):227. ... Product specificity and mechanism of protein lysine methyltransferases: Insights from the histone lysine methyltransferase SET8 ... phenylethanolamine N-methyltransferase (PNMT), histamine N-methyltransferase (HMT), and hydroxyindole o-methyltransferase ( ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex ... Protein disorder predictions are based on JRONN (Troshin, P. and Barton, G. J. unpublished), a Java implementation of RONN * ... The Protein Feature View requires a browser that supports SVG (Scalable Vector Graphics). Mouse over tracks and labels for more ... Data in red indicates combined ranges of Homology Models from SBKB and the Protein Model Portal ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex ... Protein disorder predictions are based on JRONN (Troshin, P. and Barton, G. J. unpublished), a Java implementation of RONN * ... The Protein Feature View requires a browser that supports SVG (Scalable Vector Graphics). Mouse over tracks and labels for more ... For more details on the Protein Feature view see the dedicated help page. ...
... to allow unambiguous identification of a protein.,p>,a href=/help/protein_names target=_top>More...,/a>,/p>Protein namesi. ... PROSITE; a protein domain and family database. More...PROSITEi. View protein in PROSITE. PS01131 RRNA_A_DIMETH, 1 hit. PS51689 ... Integrated resource of protein families, domains and functional sites. More...InterProi. View protein in InterPro. IPR001737 ... Simple Modular Architecture Research Tool; a protein domain database. More...SMARTi. View protein in SMART. SM00650 rADc, 1 ...
Ab162213 is a full length protein produced in Wheat germ and has been validated in WB, ELISA. Abcam… ... Proteins and Peptides. Proteomics tools. Agonists, activators, antagonists and inhibitors. Lysates. Multiplex miRNA assays. By ... The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res. 38:D142-D148 (2010) . ... Buy our Recombinant Human Methyltransferase like 5 protein. ... Recombinant-Human-Methyltransferase-like-5-protein-ab162213.pdf ...
May promote centrosome maturation probably by recruiting A-kinase anchor protein AKAP9 to centrosomes in early mitosis (PubMed: ... Putative methyltransferase C9orf114Curated (EC:2.1.1.-Curated). Alternative name(s):. Centromere protein 321 Publication. ,p> ... to allow unambiguous identification of a protein.,p>,a href=/help/protein_names target=_top>More...,/a>,/p>Protein namesi. ... section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes ...
"The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase ... "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase ... "Entrez Gene: PRMT5 protein arginine methyltransferase 5". Kim S, Gunesdogan, U, Zylicz JJ, Hackett, JA, Cougot, D, Bao, S, Lee ... Protein arginine N-methyltransferase 5 is an enzyme that in humans is encoded by the PRMT5 gene. PRMT5 symmetrically ...
... protein (histidine) methyltransferase, actin-specific histidine methyltransferase, and S-adenosyl methionine:protein-histidine ... protein-L-histidine N-tele-methyltransferase. Other names in common use include protein methylase IV, ... In enzymology, a protein-histidine N-methyltransferase (EC 2.1.1.85) is an enzyme that catalyzes the chemical reaction S- ... protein-histidine N-methyltransferase from rabbit skeletal muscle". Biochim. Biophys. Acta. 923 (1): 156-65. doi:10.1016/0304- ...
Timeline for Protein Monomethylamine methyltransferase MtmB from c.1.25.1: Monomethylamine methyltransferase MtmB: *Protein ... Family c.1.25.1: Monomethylamine methyltransferase MtmB [75099] (1 protein). *. Protein Monomethylamine methyltransferase MtmB ... Lineage for Protein: Monomethylamine methyltransferase MtmB. *Root: SCOPe 2.06 *. Class c: Alpha and beta proteins (a/b) [51349 ... Protein Monomethylamine methyltransferase MtmB from c.1.25.1: Monomethylamine methyltransferase MtmB appears in SCOPe 2.05. ...
... or on protein translation factors. This review focuses on Trm112, a small protein interacting with and activating at least four ... The last complex formed between Trm112 and Bud23 proteins modifies 18S rRNA and participates in the 40S biogenesis pathway. In ... different eukaryotic methyltransferase (MTase) enzymes modifying factors involved in translation. The Trm112-Trm9 and Trm112- ... Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus. Gabrielle ...
... recombinant proteins & enzymes, and other innovative research tools for studying Apoptosis, Metabolism, Cell Proliferation, ... BioVision develops and offers a wide variety of products including assay kits, antibodies, recombinant proteins & enzymes, and ...
... recombinant proteins & enzymes, and other innovative research tools for studying Apoptosis, Metabolism, Cell Proliferation, ... Categories: Protein Arginine Methyltransferases (PRMTs) *DNA Methyltransferases (DNMTs)(45)*Antibodies & Blocking Peptides(30) ... BioVision develops and offers a wide variety of products including assay kits, antibodies, recombinant proteins & enzymes, and ...
... from mammalian brain and erythrocytes selectively and stoichiometrically methylate peptides and proteins which contain... ... Recent findings indicate that protein carboxyl methyltransfer-ases (PCMTs) ... Modification of Isoaspartyl Peptides and Proteins by Protein Carboxyl Methyltransferase from Bovine Brain. ... Modification of Isoaspartyl Peptides and Proteins by Protein Carboxyl Methyltransferase from Bovine Brain. In: Zappia V., ...
Protein arginine methylation is catalyzed by a family of enzymes termed protein arginine methyltransferases (PRMTs) (21). The ... The protein arginine methyltransferase PRMT5 promotes D2-like dopamine receptor signaling Message Subject. (Your Name) has ... The protein arginine methyltransferase PRMT5 promotes D2-like dopamine receptor signaling. By Neah Likhite, Christopher A. ... The protein arginine methyltransferase PRMT5 promotes D2-like dopamine receptor signaling. By Neah Likhite, Christopher A. ...
Increased protein arginine methylation in chronic hypoxia: role of protein arginine methyltransferases. Yildirim, A.O., Bulau, ... Synonyms: HMT1, HRMT1L1, Histone-arginine N-methyltransferase PRMT2, MGC111373, Protein arginine N-methyltransferase 2 ... Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. Qi, C., Chang, J., Zhu, Y ... Protein Methyltransferase 2 Inhibits NF-{kappa}B Function and Promotes Apoptosis. Ganesh, L., Yoshimoto, T., Moorthy, N.C., ...
  • While the 500 kDa complex methylated predominantly myelin basic protein (MBP), the 440 kDa complex methylated hnRNP A1 protein. (nih.gov)
  • Furthermore, the amount of expressed PRMT protein, determined by Western immunoblot, did not correlate with the amount of their catalytic activity, and thus, some uncharacterized additional factor(s) may multimerize PRMTs to express catalytic activities in vivo. (nih.gov)
  • In fetal rat liver, the amount of expressed 42 kDa PRMT1 protein and the enzyme activity to methylate hnRNPA1 protein were 2- to 3-fold and 4- to 5-fold higher, respectively, than those of post-natal livers. (nih.gov)
  • Furthermore, while the PRMT1 enzyme activity increased more than 10-fold after 3 days of 70% partial hepatectomy, the amount of expressed PRMT1 protein was only about 3.2-fold higher than the control livers. (nih.gov)
  • This is a suicide reaction since the enzyme is irreversibly inactivated and the methylated protein accumulates as a dead-end product. (ebi.ac.uk)
  • In enzymology, a protein-histidine N-methyltransferase (EC 2.1.1.85) is an enzyme that catalyzes the chemical reaction S-adenosyl-L-methionine + protein L-histidine ⇌ {\displaystyle \rightleftharpoons } S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine Thus, the two substrates of this enzyme are S-adenosyl methionine and protein L-histidine, whereas its two products are S-adenosylhomocysteine and protein Ntau-methyl-L-histidine. (wikipedia.org)
  • This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. (wikipedia.org)
  • The systematic name of this enzyme class is S-adenosyl-L-methionine:protein-L-histidine N-tele-methyltransferase. (wikipedia.org)
  • In fetal rat liver, the amount of expressed 42 kDa PRMT1 protein and the enzyme activity to methylate hnRNPA1 protein were 2- to 3-fold and 4- to 5-fold higher, respectively, than those of post-natal livers. (nih.gov)
  • Furthermore, while the PRMT1 enzyme activity increased more than 10-fold after 3 days of 70% partial hepatectomy, the amount of expressed PRMT1 protein was only about 3.2-fold higher than the control livers. (nih.gov)
  • This application note describes a novel, cell-based assay platform that uses Enzyme Fragment Complementation (EFC) Technology to detect the specific binding and direct protein engagement of potential small molecule inhibitors to G9a methyltransferase and multiple bromodomain proteins. (selectscience.net)
  • Antiserum prepared against the purified folate-binding protein almost completely inactivated the enzyme activity in crude liver cytosol. (semanticscholar.org)
  • Catechol-o-methyltransferase enzyme activity and protein expression in human prefrontal cortex across the postnatal lifespan. (ox.ac.uk)
  • We examined COMT enzyme activity and protein immunoreactivity in the PFC during human postnatal development. (ox.ac.uk)
  • There was a significant 2-fold increase in COMT enzyme activity from neonate to adulthood, paralleled by increases in COMT protein immunoreactivity. (ox.ac.uk)
  • The enzyme, which is involved in methanogenesis from tetramethylammonium, catalyses the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.252, tetramethylammonium-corrinoid protein Co-methyltransferase), where it is bound to the cobalt cofactor, to coenzyme M, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis. (creative-enzymes.com)
  • This analogue is preferentially utilized by the mutant methyltransferase relative to the wild-type enzyme with a selectivity greater than 67. (scripps.edu)
  • This specific enzyme/inhibitor and enzyme/substrate design should be applicable to other members of this protein family and facilitate the characterization of protein methyltransferase function in vivo when combined with RNA expression analysis. (scripps.edu)
  • To study the biosynthesis of these compounds, especially methyl anthranilate and methyl salicylate, we identified a group of methyltransferases that are members of the SABATH enzyme family in maize ( Zea mays ). (plantphysiol.org)
  • Thiopurine methyltransferase or thiopurine S-methyltransferase ( TPMT ) is an enzyme that in humans is encoded by the TPMT gene . (wikipedia.org)
  • books.google.com - This invaluable volume, written by an international group of scientists, presents an overview of the AdoMet-dependent methyltransferases, with special emphasis on structure-function relationships.S-adenosyl-L-methionine (AdoMet) is the second most commonly used enzyme cofactor after ATP. (google.com)
  • The thirteen chapters describe in detail the structures, enzyme kinetics and biological roles of the AdoMet-dependent methyltransferases from a wide range of cell types: plant, animal, bacterial and archaeal. (google.com)
  • This protein is processed by the enzyme Taspase 1 into two fragments, MLL-C and MLL-N. These fragments reassociate and further assemble into different multiprotein complexes that regulate the transcription of specific target genes, including many of the HOX genes. (genecards.org)
  • Thus, distinct arginine methyltransferases are employed at different times of skeletal muscle differentiation for the purpose of facilitating ATP-dependent chromatin-remodeling enzyme interaction and function at myogenic genes. (umassmed.edu)
  • Furthermore, the amount of expressed PRMT protein, determined by Western immunoblot, did not correlate with the amount of their catalytic activity, and thus, some uncharacterized additional factor(s) may multimerize PRMTs to express catalytic activities in vivo. (nih.gov)
  • Despite the significant activation of canonical exercise-induced signaling involving AMP-activated protein kinase and peroxisome proliferator-activated receptor γ coactivator-1α (PGC-1α), PRMT expression and activity at the whole muscle level were unchanged. (ovid.com)
  • Here, we describe a protein arginine N -methyltransferase (PRMT), TbPRMT5, from the early-branching eukaryote Trypanosoma brucei . (asm.org)
  • Recently, protein arginine methyl transferase (PRMT) 5 expression has been closely associated with aberrant MYC function in various cancers, including brain tumors such as glioblastoma. (biomedcentral.com)
  • However, the so-called seven-β-strand (7BS) MTases, characterized by a twisted beta-sheet structure and certain conserved sequence motifs, represent the largest MTase class, and these enzymes methylate a wide range of substrates, including small metabolites, lipids, nucleic acids and proteins. (ku.dk)
  • Catechol-o-methyltransferase (COMT) alters extracellular dopamine levels in PFC, and its gene contains a functional polymorphism (Val(158)Met) that has been associated with variation in PFC function. (ox.ac.uk)
  • Furthermore, COMT protein immunoreactivity was related to Val(158)Met genotype, as has been previously demonstrated. (ox.ac.uk)
  • These methyl groups can be grafted either on nucleic acids (transfer RNA (tRNA), ribosomal RNA (rRNA), mRNA, etc.) or on protein translation factors. (mdpi.com)
  • The last complex formed between Trm112 and Bud23 proteins modifies 18S rRNA and participates in the 40S biogenesis pathway. (mdpi.com)
  • Transcriptional activation by NRs is mediated by the NR (or p160) coactivators, a family of three related 160-kD proteins that includes SRC-1, GRIP1/TIF2, and pCIP/RAC3/ACTR/AIB1/TRAM1 ( 2 ). (sciencemag.org)