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Journal Article

Human METTL16 is a N6-methyladenosine (m6A) methyltransferase that targets pre-mRNAs and various non-coding RNAs.

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Lenz,  C.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

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Supplementary Material (public)

2492773_Suppl_1.pdf
(Supplementary material), 194KB

2492773_Suppl_2.xlsx
(Supplementary material), 68KB

2492773_Suppl_3.xlsx
(Supplementary material), 17KB

2492773_Suppl_4.xlsx
(Supplementary material), 9KB

2492773_Suppl_5.pdf
(Supplementary material), 177KB

Citation

Warda, A. S., Kretschmer, J., Hackert, P., Lenz, C., Urlaub, H., Höbartner, C., et al. (2017). Human METTL16 is a N6-methyladenosine (m6A) methyltransferase that targets pre-mRNAs and various non-coding RNAs. EMBO Reports, 18(11), 2004-2014. doi:10.15252/embr.201744940.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002E-1983-5
Abstract
N6-methyladenosine (m6A) is a highly dynamic RNA modification that has recently emerged as a key regulator of gene expression. While many m6A modifications are installed by the METTL3-METTL14 complex, others appear to be introduced independently, implying that additional human m6A methyltransferases remain to be identified. Using crosslinking and analysis of cDNA (CRAC), we reveal that the putative human m6A "writer" protein METTL16 binds to the U6 snRNA and other ncRNAs as well as numerous lncRNAs and pre-mRNAs. We demonstrate that METTL16 is responsible for N6-methylation of A43 of the U6 snRNA and identify the early U6 biogenesis factors La, LARP7 and the methylphosphate capping enzyme MEPCE as METTL16 interaction partners. Interestingly, A43 lies within an essential ACAGAGA box of U6 that base pairs with 5' splice sites of pre-mRNAs during splicing, suggesting that METTL16-mediated modification of this site plays an important role in splicing regulation. The identification of METTL16 as an active m6A methyltransferase in human cells expands our understanding of the mechanisms by which the m6A landscape is installed on cellular RNAs.