The interactome of a family of potential methyltransferases in HeLa cells

Human methytransferase like proteins (METTL) are part of a large protein family characterized by the presence of binding domains for S-adenosyl methionine, a co-substrate for methylation reactions. Despite the fact that members of this protein family were shown or predicted to be DNA, RNA or protein...

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Bibliographic Details
Published in:	Scientific reports Vol. 9; no. 1; p. 6584
Main Authors:	Ignatova, Valentina V., Jansen, Pascal W. T. C., Baltissen, Marijke P., Vermeulen, Michiel, Schneider, Robert
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 29-04-2019 Nature Publishing Group
Subjects:	631/45/475 631/45/612/1238 82 82/58 82/83 Amino Acid Sequence - genetics Binding Sites - genetics Deoxyribonucleic acid DNA HeLa Cells Humanities and Social Sciences Humans Mass spectrometry Mass spectroscopy Methionine Methylation Methyltransferases - chemistry Methyltransferases - classification Methyltransferases - genetics multidisciplinary Multigene Family - genetics Protein Binding - genetics Proteins Ribonucleic acid RNA S-Adenosylmethionine - metabolism Science Science (multidisciplinary) Substrate Specificity
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Summary:	Human methytransferase like proteins (METTL) are part of a large protein family characterized by the presence of binding domains for S-adenosyl methionine, a co-substrate for methylation reactions. Despite the fact that members of this protein family were shown or predicted to be DNA, RNA or protein methyltransferases, most METTL proteins are still poorly characterized. Identification of complexes in which these potential enzymes act could help to understand their function(s) and substrate specificities. Here we systematically studied interacting partners of METTL protein family members in HeLa cells using label-free quantitative mass spectrometry. We found that, surprisingly, many of the METTL proteins appear to function outside of stable complexes whereas others including METTL7B, METTL8 and METTL9 have high-confidence interaction partners. Our study is the first systematic and comprehensive overview of the interactome of METTL protein family that can provide a crucial resource for further studies of these potential novel methyltransferases.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	2045-2322 2045-2322
DOI:	10.1038/s41598-019-43010-2