Open Access

PLoS ONE, volume 9, issue 8, pages e105394

Selenium-Based S-Adenosylmethionine Analog Reveals the Mammalian Seven-Beta-Strand Methyltransferase METTL10 to Be an EF1A1 Lysine Methyltransferase

Shimazu Tadahiro ¹

Barjau Joaquin ²

Sohtome Yoshihiro ²

Sodeoka Mikiko ²

Shinkai Yoichi ¹

Hide authors affiliations Show authors affiliations: 2 affiliations

Cellular Memory Laboratory, RIKEN, Wako, Japan |

Synthetic Organic Chemistry Laboratory, RIKEN, Wako, Japan |

Publication type: Journal Article

Publication date: 2014-08-21

Public Library of Science (PLoS)

Journal: PLoS ONE

Quartile SCImago

Quartile WOS

Impact factor: 3.7

ISSN: 19326203

DOI: 10.1371/journal.pone.0105394

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PubMed ID: 25144183

Multidisciplinary

Abstract

Lysine methylation has been extensively studied in histones, where it has been shown to provide specific epigenetic marks for the regulation of gene expression; however, the molecular mechanism and physiological function of lysine methylation in proteins other than histones remains to be fully addressed. To better understand the substrate diversity of lysine methylation, S-adenosylmethionine (SAM) derivatives with alkyne-moieties have been synthesized. A selenium-based SAM analog, propargylic Se-adenosyl-l-selenomethionine (ProSeAM), has a wide spectrum of reactivity against various lysine methyltransferases (KMTs) with sufficient stability to support enzymatic reactions in vitro. By using ProSeAM as a chemical probe for lysine methylation, we identified substrates for two seven-beta-strand KMTs, METTL21A and METTL10, on a proteomic scale in mammalian cells. METTL21A has been characterized as a heat shock protein (HSP)-70 methyltransferase. Mammalian METTL10 remains functionally uncharacterized, although its ortholog in yeast, See1, has been shown to methylate the translation elongation factor eEF1A. By using ProSeAM-mediated alkylation followed by purification and quantitative MS analysis, we confirmed that METTL21A labels HSP70 family proteins. Furthermore, we demonstrated that METTL10 also methylates the eukaryotic elongation factor EF1A1 in mammalian cells. Subsequent biochemical characterization revealed that METTL10 specifically trimethylates EF1A1 at lysine 318 and that siRNA-mediated knockdown of METTL10 decreases EF1A1 methylation levels in vivo. Thus, our study emphasizes the utility of the synthetic cofactor ProSeAM as a chemical probe for the identification of non-histone substrates of KMTs.

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Citations by journals

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Biochemical Journal	Biochemical Journal, 1, 1.25% Biochemical Journal 1 publication, 1.25%
Biochemical Society Transactions	Biochemical Society Transactions, 1, 1.25% Biochemical Society Transactions 1 publication, 1.25%
World Chinese Journal of Digestology	World Chinese Journal of Digestology, 1, 1.25% World Chinese Journal of Digestology 1 publication, 1.25%
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Frontiers in Molecular Biosciences	Frontiers in Molecular Biosciences, 1, 1.25% Frontiers in Molecular Biosciences 1 publication, 1.25%
Leukemia	Leukemia, 1, 1.25% Leukemia 1 publication, 1.25%
Journal of Cell Communication and Signaling	Journal of Cell Communication and Signaling, 1, 1.25% Journal of Cell Communication and Signaling 1 publication, 1.25%
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Fish Physiology and Biochemistry	Fish Physiology and Biochemistry, 1, 1.25% Fish Physiology and Biochemistry 1 publication, 1.25%
	2 4 6 8 10

Citations by publishers

	2 4 6 8 10 12 14 16
Springer Nature	Springer Nature, 15, 18.75% Springer Nature 15 publications, 18.75%
American Society for Biochemistry and Molecular Biology	American Society for Biochemistry and Molecular Biology, 12, 15% American Society for Biochemistry and Molecular Biology 12 publications, 15%
Wiley	Wiley, 7, 8.75% Wiley 7 publications, 8.75%
Elsevier	Elsevier, 6, 7.5% Elsevier 6 publications, 7.5%
American Chemical Society (ACS)	American Chemical Society (ACS), 5, 6.25% American Chemical Society (ACS) 5 publications, 6.25%
Multidisciplinary Digital Publishing Institute (MDPI)	Multidisciplinary Digital Publishing Institute (MDPI), 4, 5% Multidisciplinary Digital Publishing Institute (MDPI) 4 publications, 5%
Bentham Science	Bentham Science, 3, 3.75% Bentham Science 3 publications, 3.75%
Frontiers Media S.A.	Frontiers Media S.A., 3, 3.75% Frontiers Media S.A. 3 publications, 3.75%
Oxford University Press	Oxford University Press, 3, 3.75% Oxford University Press 3 publications, 3.75%
Portland Press	Portland Press, 2, 2.5% Portland Press 2 publications, 2.5%
Public Library of Science (PLoS)	Public Library of Science (PLoS), 2, 2.5% Public Library of Science (PLoS) 2 publications, 2.5%
Hindawi Limited	Hindawi Limited, 2, 2.5% Hindawi Limited 2 publications, 2.5%
eLife Sciences Publications	eLife Sciences Publications, 2, 2.5% eLife Sciences Publications 2 publications, 2.5%
Future Medicine	Future Medicine, 1, 1.25% Future Medicine 1 publication, 1.25%
Impact Journals	Impact Journals, 1, 1.25% Impact Journals 1 publication, 1.25%
IOS Press	IOS Press, 1, 1.25% IOS Press 1 publication, 1.25%
S. Karger AG	S. Karger AG, 1, 1.25% S. Karger AG 1 publication, 1.25%
Shi Jie Wei Chang Bing Xue Za Zhi She	Shi Jie Wei Chang Bing Xue Za Zhi She, 1, 1.25% Shi Jie Wei Chang Bing Xue Za Zhi She 1 publication, 1.25%
Federation of American Societies for Experimental Biology (FASEB)	Federation of American Societies for Experimental Biology (FASEB), 1, 1.25% Federation of American Societies for Experimental Biology (FASEB) 1 publication, 1.25%
Royal Society of Chemistry (RSC)	Royal Society of Chemistry (RSC), 1, 1.25% Royal Society of Chemistry (RSC) 1 publication, 1.25%
Taylor & Francis	Taylor & Francis, 1, 1.25% Taylor & Francis 1 publication, 1.25%
Cold Spring Harbor Laboratory	Cold Spring Harbor Laboratory, 1, 1.25% Cold Spring Harbor Laboratory 1 publication, 1.25%
	2 4 6 8 10 12 14 16

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Shimazu T. et al. Selenium-Based S-Adenosylmethionine Analog Reveals the Mammalian Seven-Beta-Strand Methyltransferase METTL10 to Be an EF1A1 Lysine Methyltransferase // PLoS ONE. 2014. Vol. 9. No. 8. p. e105394.

GOST all authors (up to 50) Copy

Shimazu T., Barjau J., Sohtome Y., Sodeoka M., Shinkai Y. Selenium-Based S-Adenosylmethionine Analog Reveals the Mammalian Seven-Beta-Strand Methyltransferase METTL10 to Be an EF1A1 Lysine Methyltransferase // PLoS ONE. 2014. Vol. 9. No. 8. p. e105394.

RIS |

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RIS Copy

TY - JOUR

DO - 10.1371/journal.pone.0105394

UR - https://doi.org/10.1371%2Fjournal.pone.0105394

TI - Selenium-Based S-Adenosylmethionine Analog Reveals the Mammalian Seven-Beta-Strand Methyltransferase METTL10 to Be an EF1A1 Lysine Methyltransferase

T2 - PLoS ONE

AU - Shimazu, Tadahiro

AU - Barjau, Joaquin

AU - Sohtome, Yoshihiro

AU - Sodeoka, Mikiko

AU - Shinkai, Yoichi

PY - 2014

DA - 2014/08/21 00:00:00

PB - Public Library of Science (PLoS)

SP - e105394

IS - 8

VL - 9

PMID - 25144183

SN - 1932-6203

ER -

BibTex |

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@article{2014_Shimazu,

author = {Tadahiro Shimazu and Joaquin Barjau and Yoshihiro Sohtome and Mikiko Sodeoka and Yoichi Shinkai},

title = {Selenium-Based S-Adenosylmethionine Analog Reveals the Mammalian Seven-Beta-Strand Methyltransferase METTL10 to Be an EF1A1 Lysine Methyltransferase},

journal = {PLoS ONE},

year = {2014},

volume = {9},

publisher = {Public Library of Science (PLoS)},

month = {aug},

url = {https://doi.org/10.1371%2Fjournal.pone.0105394},

number = {8},

pages = {e105394},

doi = {10.1371/journal.pone.0105394}

}

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Shimazu, Tadahiro, et al. “Selenium-Based S-Adenosylmethionine Analog Reveals the Mammalian Seven-Beta-Strand Methyltransferase METTL10 to Be an EF1A1 Lysine Methyltransferase.” PLoS ONE, vol. 9, no. 8, Aug. 2014, p. e105394. https://doi.org/10.1371%2Fjournal.pone.0105394.

Found error?

Publisher

Public Library of Science (PLoS)

Journal

PLoS ONE

Quartile SCImago

Quartile WOS

Impact factor

3.7

ISSN

19326203 (Print)