Phosphoserine inhibits neighboring arginine methylation in the RKS motif of histone H3.

Amino Acid Motifs Amino Acid Sequence Animals Arginine / chemistry Histones / chemistry Humans Methylation Molecular Dynamics Simulation Phosphoserine / chemistry Protein Processing, Post-Translational Static Electricity Xenopus laevis
Histone crosstalk Methylarginine Methylation PRMT Phosphorylation Phosphoserine Post translational modification (PTM) Symmetric arginine dimethylation (SDMA)

Journal

Archives of biochemistry and biophysics
ISSN: 1096-0384
Titre abrégé: Arch Biochem Biophys
Pays: United States
ID NLM: 0372430

Informations de publication

Date de publication:
15 02 2021
Historique:
received: 05 10 2020
revised: 13 11 2020
accepted: 28 11 2020
pubmed: 15 12 2020
medline: 20 2 2021
entrez: 14 12 2020
Statut: ppublish

Résumé

The effects of phosphorylation of histone H3 at serine 10 have been studied in the context of other posttranslational modifications such as lysine methylation. We set out to investigate the impact of phosphoserine-10 on arginine-8 methylation. We performed methylation reactions using peptides based on histone H3 that contain a phosphorylated serine and compared the extent of arginine methylation with unmodified peptides. Results obtained via fluorography indicate that peptides containing a phosphorylated serine-10 inhibit deposition of methyl groups to arginine-8 residues. To further explore the effects of phosphoserine on neighboring arginine residues, we physically characterized the non-covalent interactions between histone H3 phosphoserine-10 and arginine-8 using

Identifiants

DOI: 10.1016/j.abb.2020.108716 PMID: 33309545 PMC: PMC11028399
pubmed: 33309545
pii: S0003-9861(20)30725-6
doi: 10.1016/j.abb.2020.108716
pmc: PMC11028399
mid: NIHMS1963027
pii:
doi:

Substances chimiques

Histones 0
Phosphoserine 17885-08-4
Arginine 94ZLA3W45F

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

108716

Subventions

Organisme : NIGMS NIH HHS
ID : R25 GM061331
Pays : United States
Organisme : NIGMS NIH HHS
ID : SC2 GM118202
Pays : United States

Informations de copyright

Copyright © 2020 Elsevier Inc. All rights reserved.

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Auteurs

Juan A Leal (JA)

Department of Chemistry and Biochemistry, California State University, Los Angeles, 5151 State University Drive, Los Angeles, 90033, CA, USA.

Zoila M Estrada-Tobar (ZM)

Department of Chemistry and Biochemistry, California State University, Los Angeles, 5151 State University Drive, Los Angeles, 90033, CA, USA.

Frederick Wade (F)

Department of Physics and Astronomy, California State University, Los Angeles, 5151 State University Drive, Los Angeles, 90033, CA, USA.

Aron Judd P Mendiola (AJP)

Department of Chemistry and Biochemistry, California State University, Los Angeles, 5151 State University Drive, Los Angeles, 90033, CA, USA.

Alexander Meza (A)

Department of Chemistry and Biochemistry, California State University, Los Angeles, 5151 State University Drive, Los Angeles, 90033, CA, USA.

Mariel Mendoza (M)

Department of Chemistry and Biochemistry, California State University, Los Angeles, 5151 State University Drive, Los Angeles, 90033, CA, USA.

Paul S Nerenberg (PS)

Department of Physics and Astronomy, California State University, Los Angeles, 5151 State University Drive, Los Angeles, 90033, CA, USA; Department of Biological Sciences, California State University, Los Angeles, 5151 State University Drive, Los Angeles, 90033, CA, USA.

Cecilia I Zurita-Lopez (CI)

Department of Chemistry and Biochemistry, California State University, Los Angeles, 5151 State University Drive, Los Angeles, 90033, CA, USA. Electronic address: zuritalopez@calstatela.edu.

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Classifications MeSH

questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure secondaire des protéines › Motifs d'acides aminés › Phosphoserine inhibits neighboring arginine...
questionsmedicales.fr › Sciences de l'information › Sources d'information › Services d'information › Documentation › Données de séquences moléculaires › Séquence d'acides aminés › Phosphoserine inhibits neighboring arginine...
questionsmedicales.fr › Eucaryotes › Animaux › Phosphoserine inhibits neighboring arginine...
questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Acides aminés essentiels › Arginine › Phosphoserine inhibits neighboring arginine...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Nucléoprotéines › Histone › Phosphoserine inhibits neighboring arginine...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Phosphoserine inhibits neighboring arginine...
questionsmedicales.fr › Métabolisme › Alkylation › Méthylation › Phosphoserine inhibits neighboring arginine...
questionsmedicales.fr › Sciences de l'information › Méthodologies informatiques › Simulation numérique › Simulation de dynamique moléculaire › Phosphoserine inhibits neighboring arginine...
questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Acides phosphoaminés › Phosphosérine › Phosphoserine inhibits neighboring arginine...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › Phosphoserine inhibits neighboring arginine...
questionsmedicales.fr › Phénomènes physiques › Phénomènes magnétiques › Phénomènes électromagnétiques › Électricité › Électricité statique › Phosphoserine inhibits neighboring arginine...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Amphibiens › Anura › Pipidae › Xenopus › Xenopus laevis › Phosphoserine inhibits neighboring arginine...