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Academic literature on the topic 'Methyltransferases'

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Published: 4 June 2021
Last updated: 28 July 2024

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Journal articles on the topic "Methyltransferases"

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Wnuk, Maciej, Piotr Slipek, Mateusz Dziedzic, and Anna Lewinska. "The Roles of Host 5-Methylcytosine RNA Methyltransferases during Viral Infections." International Journal of Molecular Sciences 21, no. 21 (October 31, 2020): 8176. http://dx.doi.org/10.3390/ijms21218176.

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Eukaryotic 5-methylcytosine RNA methyltransferases catalyze the transfer of a methyl group to the fifth carbon of a cytosine base in RNA sequences to produce 5-methylcytosine (m5C). m5C RNA methyltransferases play a crucial role in the maintenance of functionality and stability of RNA. Viruses have developed a number of strategies to suppress host innate immunity and ensure efficient transcription and translation for the replication of new virions. One such viral strategy is to use host m5C RNA methyltransferases to modify viral RNA and thus to affect antiviral host responses. Here, we summarize the latest findings concerning the roles of m5C RNA methyltransferases, namely, NOL1/NOP2/SUN domain (NSUN) proteins and DNA methyltransferase 2/tRNA methyltransferase 1 (DNMT2/TRDMT1) during viral infections. Moreover, the use of m5C RNA methyltransferase inhibitors as an antiviral therapy is discussed.
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Paul, Ligi, Donald J. Ferguson, and Joseph A. Krzycki. "The Trimethylamine Methyltransferase Gene and Multiple Dimethylamine Methyltransferase Genes of Methanosarcina barkeri Contain In-Frame and Read-Through Amber Codons." Journal of Bacteriology 182, no. 9 (May 1, 2000): 2520–29. http://dx.doi.org/10.1128/jb.182.9.2520-2529.2000.

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ABSTRACT Three different methyltransferases initiate methanogenesis from trimethylamine (TMA), dimethylamine (DMA) or monomethylamine (MMA) by methylating different cognate corrinoid proteins that are subsequently used to methylate coenzyme M (CoM). Here, genes encoding the DMA and TMA methyltransferases are characterized for the first time. A single copy of mttB, the TMA methyltransferase gene, was cotranscribed with a copy of the DMA methyltransferase gene,mtbB1. However, two other nearly identical copies ofmtbB1, designated mtbB2 and mtbB3, were also found in the genome. A 6.8-kb transcript was detected with probes to mttB and mtbB1, as well as tomtbC and mttC, encoding the cognate corrinoid proteins for DMA:CoM and TMA:CoM methyl transfer, respectively, and with probes to mttP, encoding a putative membrane protein which might function as a methylamine permease. These results indicate that these genes, found on the chromosome in the ordermtbC, mttB, mttC, mttP, and mtbB1, form a single transcriptional unit. A transcriptional start site was detected 303 or 304 bp upstream of the translational start of mtbC. The MMA, DMA, and TMA methyltransferases are not homologs; however, like the MMA methyltransferase gene, the genes encoding the DMA and TMA methyltransferases each contain a single in-frame amber codon. Each of the three DMA methyltransferase gene copies from Methanosarcina barkeri contained an amber codon at the same position, followed by a downstream UAA or UGA codon. The C-terminal residues of DMA methyltransferase purified from TMA-grown cells matched the residues predicted for the gene products of mtbB1,mtbB2, or mtbB3 if termination occurred at the UAA or UGA codon rather than the in-frame amber codon. ThemttB gene from Methanosarcina thermophilacontained a UAG codon at the same position as the M. barkeri mttB gene. The UAG codon is also present in mttBtranscripts. Thus, the genes encoding the three types of methyltransferases that initiate methanogenesis from methylamine contain in-frame amber codons that are suppressed during expression of the characterized methyltransferases.
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Ramdhan, Peter, and Chenglong Li. "Targeting Viral Methyltransferases: An Approach to Antiviral Treatment for ssRNA Viruses." Viruses 14, no. 2 (February 12, 2022): 379. http://dx.doi.org/10.3390/v14020379.

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Methyltransferase enzymes have been associated with different processes within cells and viruses. Specifically, within viruses, methyltransferases are used to form the 5′cap-0 structure for optimal evasion of the host innate immune system. In this paper, we seek to discuss the various methyltransferases that exist within single-stranded RNA (ssRNA) viruses along with their respective inhibitors. Additionally, the importance of motifs such as the KDKE tetrad and glycine-rich motif in the catalytic activity of methyltransferases is discussed.
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Jeevarajah, Dharshini, John H. Patterson, Ellen Taig, Tobias Sargeant, Malcolm J. McConville, and Helen Billman-Jacobe. "Methylation of GPLs in Mycobacterium smegmatis and Mycobacterium avium." Journal of Bacteriology 186, no. 20 (October 15, 2004): 6792–99. http://dx.doi.org/10.1128/jb.186.20.6792-6799.2004.

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ABSTRACT Several species of mycobacteria express abundant glycopeptidolipids (GPLs) on the surfaces of their cells. The GPLs are glycolipids that contain modified sugars including acetylated 6-deoxy-talose and methylated rhamnose. Four methyltransferases have been implicated in the synthesis of the GPLs of Mycobacterium smegmatis and Mycobacterium avium. A rhamnosyl 3-O-methytransferase and a fatty acid methyltransferase of M. smegmatis have been previously characterized. In this paper, we characterize the methyltransferases that are responsible for modifying the hydroxyl groups at positions 2 and 4 of rhamnose and propose the biosynthetic sequence of GPL trimethylrhamnose formation. The analysis of M. avium genes through the creation of specific mutants is technically difficult; therefore, an alternative approach to determine the function of putative methyltransferases of M. avium was undertaken. Complementation of M. smegmatis methyltransferase mutants with M. avium genes revealed that MtfC and MtfB of the latter species have 4-O-methyltransferase activity and that MtfD is a 3-O-methyltransferase which can modify rhamnose of GPLs in M. smegmatis.
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Yan, Dongsheng, Yong Zhang, Lifang Niu, Yi Yuan, and Xiaofeng Cao. "Identification and characterization of two closely related histone H4 arginine 3 methyltransferases in Arabidopsis thaliana." Biochemical Journal 408, no. 1 (October 29, 2007): 113–21. http://dx.doi.org/10.1042/bj20070786.

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Arginine methylation of histone H3 and H4 plays important roles in transcriptional regulation in eukaryotes such as yeasts, fruitflies, nematode worms, fish and mammals; however, less is known in plants. In the present paper, we report the identification and characterization of two Arabidopsis thaliana protein arginine N-methyltransferases, AtPRMT1a and AtPRMT1b, which exhibit high homology with human PRMT1. Both AtPRMT1a and AtPRMT1b methylated histone H4, H2A, and myelin basic protein in vitro. Site-directed mutagenesis of the third arginine (R3) on the N-terminus of histone H4 to lysine (H4R3N) completely abolished the methylation of histone H4. When fused to GFP (green fluorescent protein), both methyltransferases localized to the cytoplasm as well as to the nucleus. Consistent with their subcellular distribution, GST (glutathione transferase) pull-down assays revealed an interaction between the two methyltransferases, suggesting that both proteins may act together in a functional unit. In addition, we demonstrated that AtFib2 (Arabidopsis thaliana fibrillarin 2), an RNA methyltransferase, is a potential substrate for AtPRMT1a and AtPRMT1b, and, furthermore, uncovered a direct interaction between the protein methyltransferase and the RNA methyltransferase. Taken together, our findings implicate AtPRMT1a and AtPRMT1b as H4-R3 protein arginine N-methyltransferases in Arabidopsis and may be involved in diverse biological processes inside and outside the nucleus.
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Lashley, Audrey, Ryan Miller, Stephanie Provenzano, Sara-Alexis Jarecki, Paul Erba, and Vonny Salim. "Functional Diversification and Structural Origins of Plant Natural Product Methyltransferases." Molecules 28, no. 1 (December 21, 2022): 43. http://dx.doi.org/10.3390/molecules28010043.

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In plants, methylation is a common step in specialized metabolic pathways, leading to a vast diversity of natural products. The methylation of these small molecules is catalyzed by S-adenosyl-l-methionine (SAM)-dependent methyltransferases, which are categorized based on the methyl-accepting atom (O, N, C, S, or Se). These methyltransferases are responsible for the transformation of metabolites involved in plant defense response, pigments, and cell signaling. Plant natural product methyltransferases are part of the Class I methyltransferase-superfamily containing the canonical Rossmann fold. Recent advances in genomics have accelerated the functional characterization of plant natural product methyltransferases, allowing for the determination of substrate specificities and regioselectivity and further realizing the potential for enzyme engineering. This review compiles known biochemically characterized plant natural product methyltransferases that have contributed to our knowledge in the diversification of small molecules mediated by methylation steps.
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Rao, Mingzhu. "Gene Expression Profile of RNA N1-methyladenosine methyltransferases." E3S Web of Conferences 218 (2020): 03052. http://dx.doi.org/10.1051/e3sconf/202021803052.

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N1-methyladenosine (m1A) is a kind of common and abundant methylation modification in eukaryotic mRNA and long-chain non-coding RNA. Nucleoside methyltransferase (MTase) of m1A is a diverse protein family, which is characterized by the presence of methyltransferases like domains and conserved S-adenosylmethionine (SAM) binding domains formed by the central sevenstranded beta-sheet structure. However, comprehensive analysis of the gene expression profile of such enzymes has not been performed to classify them according to evolutionary criteria and to guide the functional prediction. Here, we conducted extensive searches of databases to collect all members of previously identified m1A RNA methyltransferases. And we report bioinformatics studies on gene expression profile based on evolutionary analysis, sequence alignment, expression in tissues and cells within the family of RNA methyltransferases. Our analysis showed that the base modification behavior mediated by m1A RNA methyltransferases evolved from invertebrate, and the active sites of m1A RNA methyltransferases were highly conserved during the evolution from invertebrates to human. And m1A RNA methyltransferases have low tissue and cell specificity.
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Mushegian, Arcady. "Methyltransferases of Riboviria." Biomolecules 12, no. 9 (September 6, 2022): 1247. http://dx.doi.org/10.3390/biom12091247.

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Many viruses from the realm Riboviria infecting eukaryotic hosts encode protein domains with sequence similarity to S-adenosylmethionine-dependent methyltransferases. These protein domains are thought to be involved in methylation of the 5′-terminal cap structures in virus mRNAs. Some methyltransferase-like domains of Riboviria are homologous to the widespread cellular FtsJ/RrmJ-like methyltransferases involved in modification of cellular RNAs; other methyltransferases, found in a subset of positive-strand RNA viruses, have been assigned to a separate “Sindbis-like” family; and coronavirus-specific Nsp13/14-like methyltransferases appeared to be different from both those classes. The representative structures of proteins from all three groups belong to a specific variety of the Rossmann fold with a seven-stranded β-sheet, but it was unclear whether this structural similarity extends to the level of conserved sequence signatures. Here I survey methyltransferases in Riboviria and derive a joint sequence alignment model that covers all groups of virus methyltransferases and subsumes the previously defined conserved sequence motifs. Analysis of the spatial structures indicates that two highly conserved residues, a lysine and an aspartate, frequently contact a water molecule, which is located in the enzyme active center next to the methyl group of S-adenosylmethionine cofactor and could play a key role in the catalytic mechanism of the enzyme. Phylogenetic evidence indicates a likely origin of all methyltransferases of Riboviria from cellular RrmJ-like enzymes and their rapid divergence with infrequent horizontal transfer between distantly related viruses.
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BOULANGER, Marie-Chloé, Tina Branscombe MIRANDA, Steven CLARKE, Marco di FRUSCIO, Beat SUTER, Paul LASKO, and Stéphane RICHARD. "Characterization of the Drosophila protein arginine methyltransferases DART1 and DART4." Biochemical Journal 379, no. 2 (April 15, 2004): 283–89. http://dx.doi.org/10.1042/bj20031176.

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The role of arginine methylation in Drosophila melanogaster is unknown. We identified a family of nine PRMTs (protein arginine methyltransferases) by sequence homology with mammalian arginine methyltransferases, which we have named DART1 to DART9 (Drosophilaarginine methyltransferases 1–9). In keeping with the mammalian PRMT nomenclature, DART1, DART4, DART5 and DART7 are the putative homologues of PRMT1, PRMT4, PRMT5 and PRMT7. Other DART family members have a closer resemblance to PRMT1, but do not have identifiable homologues. All nine genes are expressed in Drosophila at various developmental stages. DART1 and DART4 have arginine methyltransferase activity towards substrates, including histones and RNA-binding proteins. Amino acid analysis of the methylated arginine residues confirmed that both DART1 and DART4 catalyse the formation of asymmetrical dimethylated arginine residues and they are type I arginine methyltransferases. The presence of PRMTs in D. melanogaster suggest that flies are a suitable genetic system to study arginine methylation.
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Ruszkowska, Agnieszka. "METTL16, Methyltransferase-Like Protein 16: Current Insights into Structure and Function." International Journal of Molecular Sciences 22, no. 4 (February 22, 2021): 2176. http://dx.doi.org/10.3390/ijms22042176.

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Methyltransferase-like protein 16 (METTL16) is a human RNA methyltransferase that installs m6A marks on U6 small nuclear RNA (U6 snRNA) and S-adenosylmethionine (SAM) synthetase pre-mRNA. METTL16 also controls a significant portion of m6A epitranscriptome by regulating SAM homeostasis. Multiple molecular structures of the N-terminal methyltransferase domain of METTL16, including apo forms and complexes with S-adenosylhomocysteine (SAH) or RNA, provided the structural basis of METTL16 interaction with the coenzyme and substrates, as well as indicated autoinhibitory mechanism of the enzyme activity regulation. Very recent structural and functional studies of vertebrate-conserved regions (VCRs) indicated their crucial role in the interaction with U6 snRNA. METTL16 remains an object of intense studies, as it has been associated with numerous RNA classes, including mRNA, non-coding RNA, long non-coding RNA (lncRNA), and rRNA. Moreover, the interaction between METTL16 and oncogenic lncRNA MALAT1 indicates the existence of METTL16 features specifically recognizing RNA triple helices. Overall, the number of known human m6A methyltransferases has grown from one to five during the last five years. METTL16, CAPAM, and two rRNA methyltransferases, METTL5/TRMT112 and ZCCHC4, have joined the well-known METTL3/METTL14. This work summarizes current knowledge about METTL16 in the landscape of human m6A RNA methyltransferases.
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Dissertations / Theses on the topic "Methyltransferases"

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Vidgren, Jukka. "Crystallographic studies on drug receptors catechol O-methyltransferase and carbonic anhydrase /." Lund : Dept. of Molecular Biophysics, Lund University, 1994. http://catalog.hathitrust.org/api/volumes/oclc/39725795.html.

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Vogt, Thomas. "Plant natural product glycosyl- and methyltransferases." [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=984745009.

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Cheung, Siu-ping, and 張小屏. "Genotypic and phenotypic analysis of the thiopurine S-methyltransferase (TPMT) gene with clinical correlation." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2013. http://hdl.handle.net/10722/193543.

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Immunosuppressants (such as azathioprine and 6‐mercaptopurine) are widely used in the management of patients having rheumatic diseases, inflammatory bowel diseases, hematological malignancies and organ transplant rejections. However, the adverse effects and effectiveness of these drugs are dependent on the metabolism by the enzyme, thiopurine S‐methyltransferase (TPMT), inside the body and the activity of this enzyme is determined by its genetic polymorphism. This study mainly focused on four known mutations, TPMT*2, TPMT*3A, TPMT*3B and TPMT*3C which were detected by three sets of primers, G238C, G460A and A719G targeting exons 5, 7 & 10 of the TPMT gene. Patient blood was collected from patients who had a clinical need of knowing the TPMT level (n=202). The TPMT phenotypic status of patient was determined by measuring the enzyme activity of red blood cell lysates by Enzyme‐Linked Immunosorbent Assay (ELISA) commercially available. On the other hand, the genotype was reflected by the sequencing results generated after DNA extraction from whole blood, followed by amplification, purification and DNA sequencing by the targeted primers. The majority of patients (92%) showed normal to high TPMT enzyme activity level (>17 U) and the remaining 8% was under the category of borderline activity (between 7 U to 17 U). None of them had low or deficient activity. The mean TPMT enzyme activity of all samples was 22.9 U ranging from 7.8 U to 54.1 U. No observable difference was found between male and female. The largest group of patients was having rheumatic diseases, with enzyme activity levels from 7.8 U to 54.1 U (mean of 22.8 U) which was very close to the overall findings. Also, there was no direct relationship between the lowest white blood cell count and the TPMT activity of each patient. Low white blood cell counts were not usually associated with lower TPMT enzyme activity. From the DNA sequencing results, 62.5% of the samples (n=104) had no genetic abnormalities found, 31.7% were found to have a heterozygous allele C/T and G/A at position 474 which was known to be a silent mutation with no amino acid alteration and hence was not functionally defective. Only 4.8% had heterozygous allele A/G and T/C at position 719 and one sample was found to have heterozygous allele at both positions 719 and 474. There was no significant difference in the TPMT enzymatic activity between the samples with genetic abnormalities and those without genetic abnormalities (means of TPMT enzymatic activity were 17.3 U and 21.5 U respectively, p=0.13). And also, no apparent correlation was found among the TPMT enzymatic levels, the genetic abnormalities and the disease groups. In conclusion, the individual differences in the TPMT enzyme activity were resulted from the allelic variation at the TPMT locus, it was important to fully understand the allelic variation at the TPMT gene locus. The ghenotypic analysis could be extended to the detection of all the ten exons including their spice‐site junctions and 5’ flanking promoter region of the TPMT gene by PCR single strand conformation polymorphism in future studies.
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Master of Medical Sciences
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Zheng, Sushuang. "Structure-function analyses of Encephalitozoon cuniculi : and vaccinia virus mRNA cap (guanine N-7) methyltransferases and sinefungin resistance of Saccharomyces cerevisiae /." Access full-text from WCMC, 2008. http://proquest.umi.com/pqdweb?did=1528353811&sid=5&Fmt=2&clientId=8424&RQT=309&VName=PQD.

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Bonnist, Eleanor Y. M. "The investigation of DNA-methyltransferase interactions in the adenine methyltransferases using the time-resolved fluorescence of 2-aminopurine." Thesis, University of Edinburgh, 2008. http://hdl.handle.net/1842/3175.

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The time-resolved fluorescence of 2-aminopurine (2AP) has been used to investigate DNA base flipping by the adenine methyltransferases and to study aspects of the DNA-enzyme interaction. 2AP is an excellent fluorophore to probe base flipping in the adenine methyltransferases because, as demonstrated in the present work on M.TaqI, the 2AP is delivered into the same position inside the enzyme as the natural target adenine and with the same orientation that prepares the adenine for enzyme catalysis. 2AP emits two types of fluorescence when in DNA. The first is the well-known 370-nm emission, which emanates from 2AP as a monomer species. The second is 450-nm emission and comes from a 2AP which is π-stacked with a neighbouring DNA base, a heterodimer species. Additionally, 450-nm emission is produced by a 2AP-tyrosine or 2APphenylalanine heterodimer when a flipped 2AP is π-stacked inside a DNA-methyltransferase complex. Steady state fluorescence of the 2AP-heterodimer has been used to complement the time-resolved investigations. Combined crystal- and solution-phase studies on M.TaqI have shown that when 2AP is flipped into the active site of M.TaqI it is significantly quenched by face-to-face π- stacking with the tyrosine from the NPPY catalytic motif. Not all of the flipped bases are held inside NPPY; in a minority of complexes, the flipped 2AP experiences very little quenching within the interior of the enzyme. In the sequence of bases recognised by M.TaqI, the thymine opposite the target adenine does not actively cause base flipping, as previously suggested, however, its presence aids the successful delivery of the target base into NPPY. For the DNA-M.TaqI-cofactor ternary complex, the effect of varying the cofactor has been investigated. The use of 5’-[2(amino)ethylthio]-5’-deoxyadenosine (AETA) or sinefungin as cofactor analogue causes M.TaqI to show different base flipping behaviour compared with the natural cofactor S-adenosyl-L-methionine (SAM) and with the cofactor product S-adenosyl homocysteine (SAH). In the ternary complex containing SAM the flipped base is held the most tightly within the catalytic motif. M.TaqI mutants have been studied in which the tyrosine (Y) in the NPPY motif is mutated to alanine (A) or phenylalanine (F). Stabilisation of the flipped base inside these mutants is more reliant on edge-to-face π-stacking with phenylalanine 196 and the available hydrogen-bonding in the adenine binding pocket. The NPPF-phenylalanine does not π-stack with the flipped base as NPPY-tyrosine does. Solution-phase time-resolved fluorescence studies have confirmed that M.EcoRI and M.EcoRV use a base-flipping mechanism to extrude their target bases. For M.EcoRI, with sinefungin cofactor, the majority of the flipped 2APs are not held in the NPPF catalytic motif. When the natural SAM cofactor is used, however, the flipped 2AP strongly associates with NPPF inside M.EcoRI. Non-cognate sequence binding has been investigated, in which M.EcoRI encounters a base that is in almost the same sequence context as the methylation target. M.EcoRI forms some direct contacts with the pseudo-target adenine but does not extrude the base that is in a highly stacked position inside the duplex. The H235N mutant of M.EcoRI, measured under the same conditions as the wild-type enzyme, shows different behaviour to the wild-type enzyme in a small proportion of complexes, when bound to the cognate recognition sequence, and is far more discriminating than the wild-type when bound to the non-cognate sequence. The M.EcoRV methyltransferase was found to be less efficient at flipping its target base than with M.TaqI or M.EcoRI. When M.EcoRV binds to its GATATC recognition sequence, the base-enzyme interactions of the target (GAT) and non-target (TAT) adenine position are shown to be quite different.
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May, Kyle M. "Investigation of Protein Dynamics and Communication in Adomet-Dependent Methyltransferases: Non-Ribosomal Peptide Synthetase and Protein Arginine Methyltransferase." DigitalCommons@USU, 2019. https://digitalcommons.usu.edu/etd/7550.

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For many enzymes to function correctly they must have the freedom to display a level of dynamics or communication during their catalytic cycle. The effects that protein dynamics and communication can have are wide ranging, from changes in substrate specificity or product profiles, to speed of reaction or switching activity on or off. This project investigates the protein dynamics and communication in two separate systems, a non-ribosomal peptide synthetase (NRPS), and a protein arginine methyltransferase (PRMT). PRMT1, the enzyme responsible for 80% of arginine methylation in humans, has been implicated in a variety of disease states when functioning incorrectly. For this reason, much focus has been placed on better understanding how PRMT1 determines which products it creates and at what times. This project aims to shed light on how dynamics and communication within PRMT1 dictate its activity. We have to this point developed a protocol for creating and purifying a linked PRMT1 construct which will enable us to conduct the necessary experiments capable of answering our larger questions about the PRMT1 catalytic mechanism. Our collaborators in the Zhan lab discovered the presence of a methyltransferase (Mt) in the two NRPS systems they study, which produce two different and medically relevant compounds, bassianolide and beauvericin. The Hevel lab is well suited to study methyltransferases and so were asked to help evaluate the role of these Mt domains and how they affect the production of the relevant natural products. Achieving a more complete understanding of these systems will move us closer toward the “holy grail” of being able to manipulate and harness NRPS systems for the engineering of novel medically relevant compounds. This project has found that the Mt domain substrate specificity is affected by the surrounding protein domains, or even small portions of them.
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Fellinger, Karin. "Analysis of Protein Interactions Controlling DNA Methyltransferases." Diss., lmu, 2009. http://nbn-resolving.de/urn:nbn:de:bvb:19-98919.

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Jimenez, Rosales Angelica. "Methyltransferases as bioorthogonal labelling tools for proteins." Thesis, University of Manchester, 2016. https://www.research.manchester.ac.uk/portal/en/theses/methyltransferases-as-bioorthogonal-labelling-tools-for-proteins(27231f93-7cdd-4c2d-9f31-0adc3f38b147).html.

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Development of enzymatic labelling methods has been driven by the importance of studying molecular structures and interactions to comprehend cellular processes. Methyltransferases (MTases), which regulate genetic expression by transferring a methyl group from the cofactor S-adenosyl-L-methionine (SAM) to DNA, histones and various proteins, have been shown to accept SAM analogues with an alternative alkyl group on the sulfonium centre. These alkyl groups can be transferred to the substrate, and with a further reaction can be selectively functionalized. Thus, MTases together with SAM analogues have emerged as novel labelling tools. The project aims to use MTases to obtain an orthogonal system that can selectively use a SAM cofactor analogue to transfer functional chains to proteins with a specific motif. To achieve selectivity of the system, the SAM analogue cofactor was modified on the ribose ring; to obtain a new transferase activity of the system, the transferable methyl on the sulfonium centre was changed to a different substituent. SAM analogues were produced enzymatically with hMAT2A by using 3'-deoxy-ATP and methionine or ethionine. Mutants of SET8 and novel substrates were designed to have modifications at residues in the active site, within the vicinity of the ribose ring of SAM, and were assessed for selective activity with the new analogue cofactor. The results showed that the new cofactor 3'-deoxy-S-adenosyl-L-methionine (3'dSAM) was efficient in the mono-methylation of the substrate peptide RFRKVL, and that the mutant SET8 C270V exhibited over 13 fold MTase activity in presence of 3'dSAM and the RFRKVL substrate, in comparison with the activity with the WT sequence RHRKVL and the SAM cofactor. In addition, glutathione S-transferase (GST) was used as a model protein to express the motif RFRKVL, to transform it into a potential substrate for SET8. Assessment of the MTase activity of SET8, 3'dSAM and the novel GST substrate indicated mono-methylation of the substrate. Moreover, the motif showed no interference with GST native activity. Based on the observations, a new enzymatic system shows higher selectivity with a new analogue cofactor over SAM to effectively methylate proteins expressing the consensus RFRKVL. Work on substrates, enzymes and cofactors should continue to obtain a functional-chain transferase activity of the enzymatic system.
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Burgers, Wendy Anne. "DNA methyltransferases in the regulation of transcription." Thesis, University of Cambridge, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.621269.

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Walsh, Monica Eve. "The role of SUV methyltransferases at telomeres." Thesis, The University of Sydney, 2016. http://hdl.handle.net/2123/16620.

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Telomeres are nucleoprotein structures at the ends of linear chromosomes composed of 5′-TTAGGG-3′ tandem repeat arrays, bound by histone proteins and the telomere-specific binding protein complex shelterin. In somatic cells, telomeres undergo gradual attrition with each cell division, accompanied by a loss of proliferative capacity and eventual cell death. Cancer cells are required to activate a telomere maintenance mechanism in order to circumnavigate this telomere attrition, and thereby gain unlimited proliferative capacity. This can be accomplished through the activation of the ribonucleoprotein telomerase, or through the activation of a homologous recombination (HR) mediated mechanism known as Alternative Lengthening of Telomeres (ALT). Telomere specific proteins, along with telomeric nucleosomes, cap chromosome ends to prevent them from being recognised as DNA double strand breaks. Cancers that use ALT display elevated levels of telomere-specific DNA damage response (DDR) and aberrant telomeric chromatin, implicating a role for telomere chromatin in maintaining structural integrity. Tandem repeat sequences are characterised as being highly recombinogenic. In order to prevent aberrant telomere recombination events, telomeres are maintained in a heterochromatin-like state, being enriched in the H3K9me3 and H4K20me3 heterochromatin marks. The post-translational methylation of H3K9 is achieved by the histone methyl transferase SUV39 family of proteins, which function to increase chromatin compaction. Alteration of these heterochromatin marks in mice results in the induction of ALT phenotypes. As ALT telomeres rely on a HR mechanism of telomere extension, aberrations in telomeric heterochromatin are believed to mediate HR, and therefore facilitate the growth of ALT cancers. The aim of this thesis was to explore the role of SUV39 proteins, and their heterochromatic mark H3K9me3, in maintaining telomere structural integrity. By modulating the expression of SUV39 proteins in a panel of human cancer cell lines, we were able to investigate whether telomeric chromatin state affected telomere recombination, telomere protection and telomere length maintenance. Through SUV39 depletion studies, we demonstrated that loss of H3K9me3 at telomeres results in exacerbated telomere dysfunction, detected by the association of DDR proteins at telomeres. This result revealed for the first time that heterochromatin state is important to the maintenance of telomere structure. One caveat was that this increase was only observed in cells with an already high basal level of DNA damage, implying that loss of H3K9me3 was only able to perturb telomeres with underlying structural defects. This result was independent of the employed TMM of the cell. Through SUV39 overexpression studies, we demonstrated that increased compaction resulted in a decrease in DDR at telomeres only in ALT cells, suggesting that the structural defects that underlie ALT telomeres can be supressed through increased heterochromatin. Not all ALT cell lines were able to be protected from DDR, suggesting that factors other than heterochromatin mediate the extent of telomere dysfunction at these cancer cell lines. Through depletion of the telomere capping protein, telomere repeat binding protein 2 (TRF2), we revealed that SUV39 overexpression was able to confer a protective effect in certain ALT cells. This reduction in DDR, however, could not be maintained following further telomere deprotection by the depletion of both telomere repeat binding protein 1 (TRF1) and TRF2. These results suggest that while telomeric heterochromatin may have a role in telomere DDR suppression, it is not able to confer a protective role upon exhaustive telomere insult. Overall in this thesis we demonstrated that both the depletion and overexpression of SUV39 proteins did not alter telomere length in cells which utilise either ALT or telomerase-mediated telomere extension. These findings are in direct contrast to heterochromatin-based telomere length studies carried out in both mouse and swine cell lines. Furthermore, we were able to show through chromatin immunoprecipitation studies that the SUV39 family of proteins directly associate with telomeric chromatin, albeit at a very low abundance. This result provides evidence demonstrating that there is a direct interaction between telomeres and SUV39 in human cells, but its association does not regulate telomere length.
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Books on the topic "Methyltransferases"

1

Margueron, Raphaël, and Daniel Holoch, eds. Histone Methyltransferases. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2481-4.

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G, Clarke Steven, and Tamanoi Fuyuhiko, eds. Protein methyltransferases. Amsterdam: Academic Press, 2006.

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Jeltsch, Albert, and Renata Z. Jurkowska, eds. DNA Methyltransferases - Role and Function. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-43624-1.

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Jeltsch, Albert, and Renata Z. Jurkowska, eds. DNA Methyltransferases - Role and Function. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-11454-0.

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Ki, Paik Woon, and Kim Sangduk, eds. Protein methylation. Boca Raton, Fla: CRC Press, 1990.

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F, Vani͡u︡shin B., ed. Strukturno-funkt͡s︡ionalʹnye osnovy ėnzimaticheskogo metilirovanii͡a︡ DNK. Moskva: VINITI, 1987.

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G, Chirikjian Jack, ed. Restriction endonucleases and methylases. New York: Elsevier, 1987.

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Leo, Colleen M. Thiopurine methyltransferase pharmacogenetics. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1992.

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Fitzpatrick, Teresa. Studies on the serine hydroxymethyltransferase catalysed exchange of the [alpha]-protons of amino acids. Dublin: University College Dublin, 1998.

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Henri, Grosjean, ed. DNA and RNA modification enzymes: Structure, mechanism, function, and evolution. Austin, Tex: Landes Bioscience, 2009.

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Book chapters on the topic "Methyltransferases"

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Singh, Kamaleshwar. "Methyltransferases." In Encyclopedia of Cancer, 1–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_7078-7.

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Creveling, C. R. "Methyltransferases." In Enzyme Systems that Metabolise Drugs and Other Xenobiotics, 485–99. Chichester, UK: John Wiley & Sons, Ltd, 2002. http://dx.doi.org/10.1002/0470846305.ch13.

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Singh, Kamaleshwar. "Methyltransferases." In Encyclopedia of Cancer, 2807–9. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-662-46875-3_7078.

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Erlendson, Allyson A., and Michael Freitag. "Not all Is SET for Methylation: Evolution of Eukaryotic Protein Methyltransferases." In Histone Methyltransferases, 3–40. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2481-4_1.

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Liu, Cuifang, Jicheng Zhao, and Guohong Li. "Preparation and Characterization of Chromatin Templates for Histone Methylation Assays." In Histone Methyltransferases, 91–107. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2481-4_4.

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Aflaki, Setareh, Raphaël Margueron, and Daniel Holoch. "Automated CUT & RUN Using the KingFisher Duo Prime." In Histone Methyltransferases, 253–65. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2481-4_12.

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Müller, Sebastian, Fabien Sindikubwabo, Tatiana Cañeque, and Raphaël Rodriguez. "Profiling the Regulation of Histone Methylation and Demethylation by Metabolites and Metals." In Histone Methyltransferases, 121–33. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2481-4_6.

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Servant, Nicolas. "Bioinformatics Methods for ChIP-seq Histone Analysis." In Histone Methyltransferases, 267–93. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2481-4_13.

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Larkin, Ajay, Amanda Ames, Melissa Seman, and Kaushik Ragunathan. "Investigating Mitotic Inheritance of Histone Modifications Using Tethering Strategies." In Histone Methyltransferases, 419–40. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2481-4_18.

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Tvardovskiy, Andrey, Nhuong Nguyen, and Till Bartke. "Identifying Specific Protein Interactors of Nucleosomes Carrying Methylated Histones Using Quantitative Mass Spectrometry." In Histone Methyltransferases, 327–403. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2481-4_16.

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Conference papers on the topic "Methyltransferases"

1

Kanwal, Rajnee, Manish Datt, and Sanjay Gupta. "Abstract 5258: Inhibition of DNA methyltransferases and histone methyltransferases by plant flavones." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-5258.

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Lambers, C., S. Blumer, F. Lei, A. Benazzo, K. Hoetzenecker, P. Jaksch, M. Tamm, and M. Roth. "Disease Specific Upregulation of Protein Arginine Methyltransferases in IPF." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a5276.

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Lambers, Christopher, Fang Lei, Michael Tamm, Konrad Hötzenecker, Peter Jaksch, and Michael Roth. "Disease specific upregulation of protein arginine methyltransferases in IPF." In ERS International Congress 2019 abstracts. European Respiratory Society, 2019. http://dx.doi.org/10.1183/13993003.congress-2019.pa2412.

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Huang, Steven K., Anne M. Scruggs, Bruce C. Richardson, and Marc Peters-Golden. "Regulation And Expression Of DNA Methyltransferases In Fibrotic Lung Fibroblasts." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2292.

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Kohse, Katrin, Qiongman Wang, Sabine Stritzke, Melanie Königshoff, Oliver Eickelberg, and Ali O. Yildirim. "Protein Arginine Methyltransferases (PRMT) Are Involved In Th17 Cell Differentiation." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a4399.

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Brunoir, Tessa, Chris Mulligan, Ainara Sistiaga, Khanh Vuu, Patrick Shih, Shane O'Reilly, Roger Summons, and David Gold. "STEROL METHYLTRANSFERASES IN ANNELID WORMS REWRITE THE MOLECULAR FOSSIL RECORD." In GSA Connects 2022 meeting in Denver, Colorado. Geological Society of America, 2022. http://dx.doi.org/10.1130/abs/2022am-379022.

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Harris, Victoria H., Alan Hamilton, David M. Williams, and David P. Hornby. "Studying the function of methyltransferases using nucleotide analogue based random mutagenesis." In XIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199902209.

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Ng, E., A. Kwong, W. Tsang, C. Leung, C. Wong, T. Kwok, and E. Ma. "Role of miR-143 Regulating DNA Methyltransferases 3A in Breast Cancer." In Abstracts: Thirty-Second Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 10‐13, 2009; San Antonio, TX. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-09-3148.

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Rugo, Rebecca E., James T. Mutamba, K. Naga Mohan, Tiffany Yee, J. Richard Chaillet, Joel S. Greenberger, and Bevin P. Engelward. "Abstract 171: Cell memory of a genotoxic insult is mediated by methyltransferases." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-171.

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Manning, Morenci M., Yuanyuan Jiang, Rui Wang, Lanxin Liu, Madison Bonahoom, Shomita Rode, and Zeng-Quan Yang. "Abstract A097: Genomic and transcriptomic characterization of RNA methyltransferases in breast cancer." In Abstracts: Twelfth AACR Conference on the Science of Cancer Health Disparities in Racial/Ethnic Minorities and the Medically Underserved; September 20-23, 2019; San Francisco, CA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7755.disp19-a097.

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Reports on the topic "Methyltransferases"

1

Zifeng, Li. Meta analysis of correlation between DNA methyltransferase and SLE disease activity index. INPLASY - International Platform of Registered Systematic Review Protocols, April 2020. http://dx.doi.org/10.37766/inplasy2020.4.0004.

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Ren, Ruibao. Effects of Inactivating Ras-Converting Enzyme or Isoprenylcysteine Carboxyl Methyltransferase in the Pathogenesis of Chronic Myelogenous Leukemia. Fort Belvoir, VA: Defense Technical Information Center, February 2008. http://dx.doi.org/10.21236/ada486034.

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Meiri, Noam, Michael D. Denbow, and Cynthia J. Denbow. Epigenetic Adaptation: The Regulatory Mechanisms of Hypothalamic Plasticity that Determine Stress-Response Set Point. United States Department of Agriculture, November 2013. http://dx.doi.org/10.32747/2013.7593396.bard.

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Our hypothesis was that postnatal stress exposure or sensory input alters brain activity, which induces acetylation and/or methylation on lysine residues of histone 3 and alters methylation levels in the promoter regions of stress-related genes, ultimately resulting in long-lasting changes in the stress-response set point. Therefore, the objectives of the proposal were: 1. To identify the levels of total histone 3 acetylation and different levels of methylation on lysine 9 and/or 14 during both heat and feed stress and challenge. 2. To evaluate the methylation and acetylation levels of histone 3 lysine 9 and/or 14 at the Bdnfpromoter during both heat and feed stress and challenge. 3. To evaluate the levels of the relevant methyltransferases and transmethylases during infliction of stress. 4. To identify the specific localization of the cells which respond to both specific histone modification and the enzyme involved by applying each of the stressors in the hypothalamus. 5. To evaluate the physiological effects of antisense knockdown of Ezh2 on the stress responses. 6. To measure the level of CpG methylation in the promoter region of BDNF in thermal treatments and free-fed, 12-hour fasted, and re-fed chicks during post-natal day 3, which is the critical period for feed-control establishment, and 10 days later to evaluate longterm effects. 7. The phenotypic effect of antisense “knock down” of the transmethylaseDNMT 3a. Background: The growing demand for improvements in poultry production requires an understanding of the mechanisms governing stress responses. Two of the major stressors affecting animal welfare and hence, the poultry industry in both the U.S. and Israel, are feed intake and thermal responses. Recently, it has been shown that the regulation of energy intake and expenditure, including feed intake and thermal regulation, resides in the hypothalamus and develops during a critical post-hatch period. However, little is known about the regulatory steps involved. The hypothesis to be tested in this proposal is that epigenetic changes in the hypothalamus during post-hatch early development determine the stress-response set point for both feed and thermal stressors. The ambitious goals that were set for this proposal were met. It was established that both stressors i.e. feed and thermal stress, can be manipulated during the critical period of development at day 3 to induce resilience to stress later in life. Specifically it was established that unfavorable nutritional conditions during early developmental periods or heat exposure influences subsequent adaptability to those same stressful conditions. Furthermore it was demonstrated that epigenetic marks on the promoter of genes involved in stress memory are altered both during stress, and as a result, later in life. Specifically it was demonstrated that fasting and heat had an effect on methylation and acetylation of histone 3 at various lysine residues in the hypothalamus during exposure to stress on day 3 and during stress challenge on day 10. Furthermore, the enzymes that perform these modifications are altered both during stress conditioning and challenge. Finally, these modifications are both necessary and sufficient, since antisense "knockdown" of these enzymes affects histone modifications, and as a consequence stress resilience. DNA methylation was also demonstrated at the promoters of genes involved in heat stress regulation and long-term resilience. It should be noted that the only goal that we did not meet because of technical reasons was No. 7. In conclusion: The outcome of this research may provide information for the improvement of stress responses in high yield poultry breeds using epigenetic adaptation approaches during critical periods in the course of early development in order to improve animal welfare even under suboptimum environmental conditions.
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