Expression of the mRNA (N6-adenosine)-methyltransferase S-adenosyl-?-methionine binding subunit mRNA in cultured cells

Leach, Richard A.; Tuck, Martin T.

doi:10.1016/s1357-2725(01)00071-1

Cited by 13 publications

(11 citation statements)

References 45 publications

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“…Cultured cancer cells have an increased ratio of the longer MT-A70 splice variant relative to the shorter form (Leach and Tuck, 2001). This is consistent with the observation that extracts of immortalized human and mouse cell lines have an increased mRNA N 6 -adenosine methyltransferase activity (Tuck et al, 1996).…”

Section: Tlc Detection Of M 6 a In Arabidopsis Tissuessupporting

confidence: 87%

MTA Is an Arabidopsis Messenger RNA Adenosine Methylase and Interacts with a Homolog of a Sex-Specific Splicing Factor

et al. 2008

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N 6 -Methyladenosine is a ubiquitous modification identified in the mRNA of numerous eukaryotes, where it is present within both coding and noncoding regions. However, this base modification does not alter the coding capacity, and its biological significance remains unclear. We show that Arabidopsis thaliana mRNA contains N 6 -methyladenosine at levels similar to those previously reported for animal cells. We further show that inactivation of the Arabidopsis ortholog of the yeast and human mRNA adenosine methylase (MTA) results in failure of the developing embryo to progress past the globular stage. We also demonstrate that the arrested seeds are deficient in mRNAs containing N 6 -methyladenosine. Expression of MTA is strongly associated with dividing tissues, particularly reproductive organs, shoot meristems, and emerging lateral roots. Finally, we show that MTA interacts in vitro and in vivo with At FIP37, a homolog of the Drosophila protein FEMALE LETHAL2D and of human WILMS' TUMOUR1-ASSOCIATING PROTEIN. The results reported here provide direct evidence for an essential function for N 6 -methyladenosine in a multicellular eukaryote, and the interaction with At FIP37 suggests possible RNA processing events that might be regulated or altered by this base modification.

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Section: Tlc Detection Of M 6 a In Arabidopsis Tissuessupporting

confidence: 87%

MTA Is an Arabidopsis Messenger RNA Adenosine Methylase and Interacts with a Homolog of a Sex-Specific Splicing Factor

et al. 2008

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“…Furthermore, the localization of METTL3 seen using different antibodies showed a granular cytoplasmic staining or perinuclear staining 67 , and immunostaining for the Drosophila homologue, IME4, indicated some immunoreactivity in the cytoplasm 59 . Notably, METTL3 is expressed as both long and short alternatively spliced isoforms, which remain to be characterized 68, 69 . Conceivably, some of the variability in the staining and localization may reflect these isoforms.…”

Section: Enzymes That Mediate M6amethylationmentioning

confidence: 99%

The dynamic epitranscriptome: N6-methyladenosine and gene expression control

Meyer

Jaffrey

2014

Nat Rev Mol Cell Biol

854

991

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N6-methyladenosine (m6A) is a modified base that has long been known to be present in noncoding RNAs, ribosomal RNA, polyadenylated RNA and at least one mammalian mRNA. However, our understanding of the prevalence of this modification has been fundamentally redefined by transcriptome-wide m6A mapping studies, which have shown that m6A is present in a large subset of the transcriptome in specific regions of mRNA. This suggests that mRNA may undergo post-transcriptional methylation to regulate its fate and function, analogous to methyl modifications in DNA. Thus, the pattern of methylation constitutes an mRNA ‘epitranscriptome’. The identification of adenosine methyltransferases (‘writers’), m6A demethylating enzymes (‘erasers’) and m6A binding proteins (‘readers’) is helping to define cellular pathways for the post-transcriptional regulation of mRNAs.

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“…Two functional domains responsible for methylation activity have been identified in human METTL3 including consensus methylation motif I (CM I), which is the Adomet-binding domain, and CM II that contains catalytic residues for methylation activity (Figure 1; Figure 2 A ). Two isoforms of METTL3 have been discovered and the ratio of their expression varies greatly among tissues or cell types, suggesting distinct biological functions for each of them [42].…”

Section: M6a Methyltransferasementioning

confidence: 99%

N6-Methyl-Adenosine (m6A) in RNA: An Old Modification with A Novel Epigenetic Function

Niu

Yong-sheng

et al. 2012

Genomics, Proteomics &Amp; Bioinformatics

389

305

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N6-methyl-adenosine (m6A) is one of the most common and abundant modifications on RNA molecules present in eukaryotes. However, the biological significance of m6A methylation remains largely unknown. Several independent lines of evidence suggest that the dynamic regulation of m6A may have a profound impact on gene expression regulation. The m6A modification is catalyzed by an unidentified methyltransferase complex containing at least one subunit methyltransferase like 3 (METTL3). m6A modification on messenger RNAs (mRNAs) mainly occurs in the exonic regions and 3′-untranslated region (3′-UTR) as revealed by high-throughput m6A-seq. One significant advance in m6A research is the recent discovery of the first two m6A RNA demethylases fat mass and obesity-associated (FTO) gene and ALKBH5, which catalyze m6A demethylation in an α-ketoglutarate (α-KG)- and Fe2+-dependent manner. Recent studies in model organisms demonstrate that METTL3, FTO and ALKBH5 play important roles in many biological processes, ranging from development and metabolism to fertility. Moreover, perturbation of activities of these enzymes leads to the disturbed expression of thousands of genes at the cellular level, implicating a regulatory role of m6A in RNA metabolism. Given the vital roles of DNA and histone methylations in epigenetic regulation of basic life processes in mammals, the dynamic and reversible chemical m6A modification on RNA may also serve as a novel epigenetic marker of profound biological significances.

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Expression of the mRNA (N6-adenosine)-methyltransferase S-adenosyl-?-methionine binding subunit mRNA in cultured cells

Cited by 13 publications

References 45 publications

MTA Is an Arabidopsis Messenger RNA Adenosine Methylase and Interacts with a Homolog of a Sex-Specific Splicing Factor

MTA Is an Arabidopsis Messenger RNA Adenosine Methylase and Interacts with a Homolog of a Sex-Specific Splicing Factor

The dynamic epitranscriptome: N6-methyladenosine and gene expression control

N6-Methyl-Adenosine (m6A) in RNA: An Old Modification with A Novel Epigenetic Function

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