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Role of Histone Methyltransferase in Breast Cancer
Published in Meenu Gupta, Rachna Jain, Arun Solanki, Fadi Al-Turjman, Cancer Prediction for Industrial IoT 4.0: A Machine Learning Perspective, 2021
Surekha Manhas, Zaved Ahmed Khan
However, G9a displays its action as histone protein, such as lysine methyltransferase. Numerous studies have described G9a as also having the potential to methylate various other non-protein targets, which include G9a itself, p53, SIRT1, p21, Reptin, MyoD, WIZ and ACINUS, CDYL1, C/EBPβ, and range of numerous non-histone based targets, such as G9a itself [110], CDYL1, ACINUS, C/EBPβ, WIZ histone deacetylase (HDAC)1, CSB, KLF12, and mAM [118]. Moreover, the precise posttranslational methylation role on the protein’s function remains unclear; non-histone protein methylation might affect protein-based interactions, protein stability, subcellular localization, and subcellular function [119].
Protein Carboxyl Methylation and Sperm Motility
Published in Claude Gagnon, Controls of Sperm Motility, 2020
Direct evidence for a role for protein-carboxyl methylation in physiological conditions is still lacking. Recent in vitro studies with peptides and proteins by the groups of Clarke and Aswad8,10,69-71 strongly suggest that methylation by PCM occurs on isoaspartyl residues that are spontaneously formed from deamidated asparaginyl residues. It was suggested that PCM action on these abnormal residues could serve: (1) as a repair mechanism in which the isoaspartyl residues would be transformed into normal l-aspartyl residues, (2) as a tag to identify a protein as a substrate for a catabolic enzyme, or (3) as a regulatory mechanism of protein function. The low stochiometry of protein methylation in most native proteins is consistent with the first two hypotheses. On the other hand, the observation that the nuclear matrix protein lamin B is stoichiometrically methylated in intact cells and that the extent of this methylation varies during the cell cycle72 support the third hypothesis since the incidence of isoaspartyl residues in proteins is less than 1%.8
N-Methylation and N-Acetylation of Nonhistone Chromosomal Proteins
Published in Lubomir S. Hnilica, Chromosomal Nonhistone Proteins, 2018
Methylation of proteins and particularly that of histones, has been the subject of much research, and has been reviewed by Hnilica in The Structure and Biological Function of Histones; the first book in this series. Protein methylation in general, including that of histones, has been reviewed comprehensively by Paik and Kim.1,2 This review will therefore, be confined to N-methylation of NHC proteins.
Zinc affects nuclear factor kappa b and DNA methyltransferase activity in C3H cancer fibroblast cells induced by a 2100 MHz electromagnetic field
Published in Electromagnetic Biology and Medicine, 2022
D. Duzgun Ergun, N. Pastaci Ozsobaci, T. Yilmaz, D. Ozcelik, M. T. Kalkan
Epigenetic changes play an important role in tumor development and progression by affecting the pathways related to tumor development in cancer cells. Methylation, defined as the addition of a methyl group to a chemical compound, is a reaction that ensures the normal regulation and development of the genome. Methylation regulates gene expression by playing a role in epigenetic events such as gene activation, repression and chromatin remodeling. In biological systems, methylation occurs in two ways: DNA methylation and protein methylation. DNA methylation occurs by the binding of a methyl group (CH3) to the fifth carbon (C) atom of cytosine at the CpG (cytosine, phosphate, guanine) site via DNA methyltransferases (DNMTs) (Brito et al. 2020; Jarosz et al. 2017). There are three DNMTs in mammals: DNMT1, DNMT3A and DNMT3B. The pattern of DNA methylation is associated with under- or over-expression of some proteins and may cause pathologies such as obesity, cardiovascular, neurogenetic, renal and psychiatric disorders, and cancer in particular. Epigenetic mechanisms can be modified to prevent cancer development and DNMT inhibitors have an important place in the development of new therapeutic agents. The DNMT inhibitors can reverse epigenetic changes through induction of apoptosis, and anti-proliferative activity in cancer cells and are considered targets in cancer treatment. The DNMT inhibitors combined with various dietary supplements can exert an anti-proliferative effect on cancer cells (Coley 2008; Gros et al. 2012).
High-throughput tool to discriminate effects of NMs (Cu-NPs, Cu-nanowires, CuNO3, and Cu salt aged): transcriptomics in Enchytraeus crypticus
Published in Nanotoxicology, 2018
Susana I. L. Gomes, Carlos P. Roca, Natália Pegoraro, Tito Trindade, Janeck J. Scott-Fordsmand, Mónica J. B. Amorim
Copper, independently of the form, affected several protein post-transcriptional modifications, i.e. methylation, alkylation (methylation is the most common type of alkylation) and ubiquitination, via the up-regulation of several transcripts including methyltransferases (e.g. protein arginine methyltransferase 1 and 7) and ubiquitin conjugating enzymes (for protein ubiquitination), as the ubiquitin-conjugating enzyme e2n (qPCR confirmed). Both protein methylation and ubiquitination play important roles in the regulation of intracellular signaling events (Paik, Paik, and Kim 2007; Komander 2009), in addition methylation is involved in chromatin remodeling, which has been linked with epigenetics (Molina-Serrano, Schiza, and Kirmizis 2013). It is not clear how these post-transcriptional modifications can further impact organisms, however, based on this, longer-term and transgenerational effects should be investigated.
Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2020
Anna Di Fiore, Claudiu T. Supuran, Andrea Scaloni, Giuseppina De Simone
Protein methylation is a PTM featuring the addition of methyl groups to proteins. Generally, it affects the side-chain of R and K residues120. The former can be methylated once (monomethylated R) or twice (dimethylated R) by different classes of protein R methyltransferases (PRMTs). The latter can be methylated once, twice, or three times by protein K methyltransferases (PKMTs). Similarly to phosphorylation, methylation can introduce a net charge on the amino acid side chain, possibly affecting the interaction of proteins. Thus, this process can regulate different biological processes.