《Table 1m6A writer proteins and homologs across different species》

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《Structural Insights into N~6-methyladenosine (m~6A) Modification in the Transcriptome》

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Note:At MTA，m RNA adenosine methylase in Arabidopsis thaliana；At MTB，ortholog of human METTL14 in Arabidopsis thaliana；FIP37，FKBP12-interacting protein of 37 k Da；Fl（2）d，female-lethal（2）d；HAKAI，E3 ubiquitin-protein ligase Hakai；Ime4，inducer of me

The enzyme that catalyzes the m6A modification was first isolated in the 1990s[57，58].Rottman and colleagues identified at least two separate protein factors，methyltransferase component A（MT-A）and MT-B，both of which are able to install m6A in m RNA.One component of the MT-A complex，the S-adenosylmethionine（SAM or Ado Met）-binding site on a70-k Da subunit（MT-A70），was characterized as a key subunit of methyltransferase[58].Lately，MT-A70 was assigned as methyltransferase-like 3（METTL3）by the Human Genome Organization（HUGO）Gene Nomenclature Committee[59].In all the organisms that have been examined so far，an induced experimental deficiency of METTL3 or its homologs leads to apoptosis[37]，defects in gametogenesis[60]，and embryonic lethality[23].In 2014，several groups independently revealed that METTL3 interacts with METTL14 to form a stable complex[52–55]，which deposits m6A on m RNAs.According to phylogenetic analyses of the MT-A70 family，METTL14 is a homolog of METTL3[61，62].Both of these homologs possess a methyltransferase domain（MTase domain or MTD）（Figure 1A） ，a consensus fold in the methyltransferase family[61，62].Knockdown of METTL3 and METTL14dramatically reduces m6A levels in mammalian cells[52，53].The METTL3–METTL14 complex exhibits significantlyincreased methyltransferase activity in vitro compared to each individual protein alone[52，53，63，64].Thus，both METTL3and METTL14 are core components of the m6A writer complex（Figure 1B and Table 1）.