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Polyphosphate attachment to lysine repeats is a non-covalent protein modification.
Neville, Nolan; Lehotsky, Kirsten; Klupt, Kody A; Downey, Michael; Jia, Zongchao.
Afiliação
  • Neville N; Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.
  • Lehotsky K; Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.
  • Klupt KA; Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.
  • 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.
  • Jia Z; Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada. Electronic address: jia@queensu.ca.
Mol Cell ; 84(9): 1802-1810.e4, 2024 May 02.
Article em En | MEDLINE | ID: mdl-38701741
ABSTRACT
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 31P NMR. Ionic interaction with lysine residues alone is sufficient for polyP modification, and we present a new list of non-PASK lysine repeat proteins that undergo polyP modification. This work clarifies the biochemistry of polyP-lysine modification, with important implications for both studying and modulating this phenomenon. This Matters Arising paper is in response to Azevedo et al. (2015), published in Molecular Cell. See also the Matters Arising Response by Azevedo et al. (2024), published in this issue.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ácidos Fosfóricos / Polifosfatos / Amidas / Lisina Limite: Humans Idioma: En Revista: Mol Cell Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Canadá

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ácidos Fosfóricos / Polifosfatos / Amidas / Lisina Limite: Humans Idioma: En Revista: Mol Cell Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Canadá