Intrinsic catalytic properties of histone H3 lysine-9 methyltransferases preserve monomethylation levels under low S-adenosylmethionine.

Methyltransferases / genetics Histones / metabolism S-Adenosylmethionine / metabolism Lysine / metabolism Histone-Lysine N-Methyltransferase / metabolism Methylation
S-adenosylmethionine histone kinetics metabolism methyltransferase nucleosome

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
07 2023
Historique:
received: 18 05 2023
revised: 10 06 2023
accepted: 13 06 2023
medline: 31 7 2023
pubmed: 19 6 2023
entrez: 18 6 2023
Statut: ppublish

Résumé

S-adenosylmethionine (SAM) is the methyl donor for site-specific methylation reactions on histone proteins, imparting key epigenetic information. During SAM-depleted conditions that can arise from dietary methionine restriction, lysine di- and tri-methylation are reduced while sites such as Histone-3 lysine-9 (H3K9) are actively maintained, allowing cells to restore higher-state methylation upon metabolic recovery. Here, we investigated if the intrinsic catalytic properties of H3K9 histone methyltransferases (HMTs) contribute to this epigenetic persistence. We employed systematic kinetic analyses and substrate binding assays using four recombinant H3K9 HMTs (i.e., EHMT1, EHMT2, SUV39H1, and SUV39H2). At both high and low (i.e., sub-saturating) SAM, all HMTs displayed the highest catalytic efficiency (k

Identifiants

DOI: 10.1016/j.jbc.2023.104938 PMID: 37331600 PMC: PMC10404681
pubmed: 37331600
pii: S0021-9258(23)01966-X
doi: 10.1016/j.jbc.2023.104938
pmc: PMC10404681
pii:
doi:

Substances chimiques

Methyltransferases EC 2.1.1.-
Histones 0
S-Adenosylmethionine 7LP2MPO46S
Lysine K3Z4F929H6
Histone-Lysine N-Methyltransferase EC 2.1.1.43

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

104938

Subventions

Organisme : NIGMS NIH HHS
ID : R37 GM059785
Pays : United States

Informations de copyright

Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest J. M. D. is cofounder of Galilei Biosciences and consults for Evrys Bio.

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Auteurs

Spencer A Haws (SA)

Wisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, Wisconsin, USA; Department of Biomolecular Chemistry, SMPH, University of Wisconsin-Madison, Madison, Wisconsin, USA.

Lillian J Miller (LJ)

Wisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, Wisconsin, USA; Department of Biomolecular Chemistry, SMPH, University of Wisconsin-Madison, Madison, Wisconsin, USA.

Diego Rojas La Luz (DR)

Department of Mathematics, University of Wisconsin-Madison, Madison, Wisconsin, USA.

Vyacheslav I Kuznetsov (VI)

Wisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, Wisconsin, USA; Department of Biomolecular Chemistry, SMPH, University of Wisconsin-Madison, Madison, Wisconsin, USA.

Raymond C Trievel (RC)

Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA.

Gheorghe Craciun (G)

Department of Biomolecular Chemistry, SMPH, University of Wisconsin-Madison, Madison, Wisconsin, USA; Department of Mathematics, University of Wisconsin-Madison, Madison, Wisconsin, USA.

John M Denu (JM)

Wisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, Wisconsin, USA; Department of Biomolecular Chemistry, SMPH, University of Wisconsin-Madison, Madison, Wisconsin, USA. Electronic address: john.denu@wisc.edu.

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Classifications MeSH

questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › One-carbon group transferases › Methyltransferases › Intrinsic catalytic properties of histone H3...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Nucléoprotéines › Histone › Intrinsic catalytic properties of histone H3...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Nucléosides › Ribonucléosides › Adénosine › Adémétionine › Intrinsic catalytic properties of histone H3...
questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Acides aminés essentiels › Lysine › Intrinsic catalytic properties of histone H3...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › One-carbon group transferases › Methyltransferases › Protein Methyltransferases › Histone méthyltransférases › Histone-lysine N-methyltransferase › Intrinsic catalytic properties of histone H3...
questionsmedicales.fr › Métabolisme › Alkylation › Méthylation › Intrinsic catalytic properties of histone H3...