The interactome of a family of potential methyltransferases in HeLa cells
2019-04-29
Valentina V. Ignatova, Pascal W. T. C. Jansen, Marijke P. Baltissen, Michiel Vermeulen & Robert Schneider
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.
Speaker: Prof. Dr. Thomas Carell
Ludwig-Maximilians-Universität München
Institut für Chemische Epigenetik (ICEM)
Department of Chemistry
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Germany
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Management: Dr. Nada Raddaoui
Institute for Chemical Epigenetics Munich (ICEM)
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Würmtalstrasse 201, Building L, Room 03.004
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Germany
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Secretary: Birgit Carell
Institute for Chemical Epigenetics Munich (ICEM)
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Würmtalstrasse 201, Building L, Room 00.007
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Germany
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website support: Martina Schuster
Prof. Dr. Lena Daumann
LMU Munich
Department of Chemistry
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Dr. Sabine Schneider
LMU Munich
Institute for Chemical Epigenetics
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Dr. Martin Sumser (Coordinator)
LMU Munich
Institute for Chemical Epigenetics
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81377 Munich, Germany
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