The Inhibition of the Mammalian DNA Methyltransferase 3a (Dnmt3a) by Dietary Black Tea and Coffee Polyphenols

2015 ◽  
pp. 213-231
Author(s):  
Arumugam Rajavelu ◽  
Zumrad Tulyasheva ◽  
Rakesh Jaiswal ◽  
Albert Jeltsch ◽  
Nikolai Kuhnert
Keyword(s):  
Dna Methyltransferase ◽  
Black Tea ◽  
Dna Methyltransferase 3A

scholarly journals The inhibition of the mammalian DNA methyltransferase 3a (Dnmt3a) by dietary black tea and coffee polyphenols

2011 ◽  
Vol 12 (1) ◽  
pp. 16 ◽  
Author(s):  
Arumugam Rajavelu ◽  
Zumrad Tulyasheva ◽  
Rakesh Jaiswal ◽  
Albert Jeltsch ◽  
Nikolai Kuhnert
Keyword(s):  
Dna Methyltransferase ◽  
Black Tea ◽  
Dna Methyltransferase 3A

scholarly journals DNA methyltransferase 3a mediates developmental thermal plasticity

BMC Biology ◽  
2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Isabella Loughland ◽  
Alexander Little ◽  
Frank Seebacher
Keyword(s):  
Environmental Change ◽  
Dna Methyltransferase ◽  
Developmental Plasticity ◽  
Citrate Synthase ◽  
Thermal Sensitivity ◽  
Short Term ◽  
Cold Temperatures ◽  
Knock Out ◽  
Thermal Plasticity ◽  
Dna Methyltransferase 3A

Abstract Background Thermal plasticity is pivotal for evolution in changing climates and in mediating resilience to its potentially negative effects. The efficacy to respond to environmental change depends on underlying mechanisms. DNA methylation induced by DNA methyltransferase 3 enzymes in the germline or during early embryonic development may be correlated with responses to environmental change. This developmental plasticity can interact with reversible acclimation within adult organisms, which would increase the speed of response and could alleviate potential mismatches between parental or early embryonic environments and those experienced at later life stages. Our aim was to determine whether there is a causative relationship between DNMT3 enzyme and developmental thermal plasticity and whether either or both interact with short-term acclimation to alter fitness and thermal responses in zebrafish (Danio rerio). Results We developed a novel DNMT3a knock-out model to show that sequential knock-out of DNA methyltransferase 3a isoforms (DNMT3aa−/− and DNMT3aa−/−ab−/−) additively decreased survival and increased deformities when cold developmental temperatures in zebrafish offspring mismatched warm temperatures experienced by parents. Interestingly, short-term cold acclimation of parents before breeding rescued DNMT3a knock-out offspring by restoring survival at cold temperatures. DNMT3a knock-out genotype interacted with developmental temperatures to modify thermal performance curves in offspring, where at least one DNMT3a isoform was necessary to buffer locomotion from increasing temperatures. The thermal sensitivity of citrate synthase activity, an indicator of mitochondrial density, was less severely affected by DNMT3a knock-out, but there was nonetheless a significant interaction between genotype and developmental temperatures. Conclusions Our results show that DNMT3a regulates developmental thermal plasticity and that the phenotypic effects of different DNMT3a isoforms are additive. However, DNMT3a interacts with other mechanisms, such as histone (de)acetylation, induced during short-term acclimation to buffer phenotypes from environmental change. Interactions between these mechanisms make phenotypic compensation for climate change more efficient and make it less likely that thermal plasticity incurs a cost resulting from environmental mismatches.

scholarly journals Inhibition of intestinal tumor formation by deletion of the DNA methyltransferase 3a

Oncogene ◽  
2014 ◽  
Vol 34 (14) ◽  
pp. 1822-1830 ◽  
Author(s):  
B Weis ◽  
J Schmidt ◽  
H Maamar ◽  
A Raj ◽  
H Lin ◽  
...  
Keyword(s):  
Dna Methyltransferase ◽  
Tumor Formation ◽  
Intestinal Tumor ◽  
Dna Methyltransferase 3A

scholarly journals Identification of transcription termination defects at DNA hypomethylated transcription termination sites in DNA methyltransferase 3a-deficient vertebrates.

2021 ◽  
Author(s):  
Masaki Shirai ◽  
Takuya Nara ◽  
Haruko Takahashi ◽  
Kazuya Takayama ◽  
Yuan Chen ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Dna Methyltransferase ◽  
De Novo ◽  
Es Cells ◽  
Transcription Termination ◽  
Promoter Regions ◽  
Zebrafish Model ◽  
Body Regions ◽  
Chimeric Transcripts ◽  
Dna Methyltransferase 3A

CpG methylation in genomic DNA is well known as a repressive epigenetic marker in eukaryotic transcription, and DNA methylation of the promoter regions is correlated with silencing of gene expression. In contrast to the promoter regions, the function of DNA methylation during transcription termination remains to be elucidated. A recent study has revealed that mouse DNA methyltransferase 3a (Dnmt3a) mainly functions in de novo methylation in the promoter and gene body regions (including transcription termination sites (TTSs)) during development. To investigate the relationship between DNA methylation overlapping the TTSs and transcription termination, we employed two strategies: informatic analysis using already deposited datasets of Dnmt3a-/- mouse cells and the zebrafish model system. Bioinformatic analysis using methylome and transcriptome data showed that hypomethylated differentially methylated regions overlapping the TTSs were associated with increased read counts and chimeric transcripts downstream of TTSs in Dnmt3a-/- Agouti-related protein neurons, but not in Dnmt3a-/- ES cells and MEFs. We experimentally detected increased read-through and chimeric transcripts downstream of hypomethylated TTSs in zebrafish maternal-zygotic dnmt3aa-/- mutants. This study is the first to identify transcription termination defects in DNA hypomethylated TTSs in Dnmt3a-/- vertebrates.

Analysis of DNA methyltransferase 3A gene mutations in patients with Philadelphia-negative myeloproliferative neoplasms

2017 ◽  
Vol 6 (1) ◽  
pp. 81
Author(s):  
Najmaldin Saki ◽  
Neda Ketabchi ◽  
Mostafa Paridar ◽  
Javad Mohammadi-Asl ◽  
Alireza Abooali ◽  
...  
Keyword(s):  
Dna Methyltransferase ◽  
Myeloproliferative Neoplasms ◽  
Gene Mutations ◽  
Dna Methyltransferase 3A
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