Polyphosphate attachment to lysine repeats is a non-covalent protein modification.

Lysine / metabolism Polyphosphates / chemistry Phosphorylation Humans Protein Processing, Post-Translational Proteins / chemistry Amides Phosphoric Acids
Nsr1 Rts1 Top1 lysine polyphosphorylation phosphoramidate polyphosphate post-translational modification

Journal

Molecular cell
ISSN: 1097-4164
Titre abrégé: Mol Cell
Pays: United States
ID NLM: 9802571

Informations de publication

Date de publication:
02 May 2024
Historique:
received: 19 10 2023
revised: 12 03 2024
accepted: 29 03 2024
medline: 4 5 2024
pubmed: 4 5 2024
entrez: 3 5 2024
Statut: ppublish

Résumé

Polyphosphate (polyP) is a chain of inorganic phosphate that is present in all domains of life and affects diverse cellular phenomena, ranging from blood clotting to cancer. A study by Azevedo et al. described a protein modification whereby polyP is attached to lysine residues within polyacidic serine and lysine (PASK) motifs via what the authors claimed to be covalent phosphoramidate bonding. This was based largely on the remarkable ability of the modification to survive extreme denaturing conditions. Our study demonstrates that lysine polyphosphorylation is non-covalent, based on its sensitivity to ionic strength and lysine protonation and absence of phosphoramidate bond formation, as analyzed via

Identifiants

DOI: 10.1016/j.molcel.2024.03.028 PMID: 38701741
pubmed: 38701741
pii: S1097-2765(24)00277-6
doi: 10.1016/j.molcel.2024.03.028
pii:
doi:

Substances chimiques

Lysine K3Z4F929H6
Polyphosphates 0
Proteins 0
phosphoramidic acid 9Q189608GB
Amides 0
Phosphoric Acids 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1802-1810.e4

Informations de copyright

Copyright © 2024 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

Auteurs

Nolan Neville (N)

Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.

Kirsten Lehotsky (K)

Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.

Kody A Klupt (KA)

Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.

Michael Downey (M)

Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada; Ottawa Institute of Systems Biology, Ottawa, ON K1H 8M5, Canada.

Zongchao Jia (Z)

Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada. Electronic address: jia@queensu.ca.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Acides aminés essentiels › Lysine › Polyphosphate attachment to lysine repeats is...
questionsmedicales.fr › Produits chimiques inorganiques › Composés du phosphore › Acides du phosphore › Acides phosphoriques › Phosphates › Polyphosphates › Polyphosphate attachment to lysine repeats is...
questionsmedicales.fr › Métabolisme › Phosphorylation › Polyphosphate attachment to lysine repeats is...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Polyphosphate attachment to lysine repeats is...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › Polyphosphate attachment to lysine repeats is...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Polyphosphate attachment to lysine repeats is...
questionsmedicales.fr › Composés chimiques organiques › Amides › Polyphosphate attachment to lysine repeats is...
questionsmedicales.fr › Produits chimiques inorganiques › Composés du phosphore › Acides du phosphore › Acides phosphoriques › Polyphosphate attachment to lysine repeats is...