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Poster De Conférence Année : 2022

N-terminal acetylation status of nuclear proteins upon proteotoxic stress

Yuliya Kuchkovska
  • Fonction : Auteur
Jean-Baptiste Boyer
Thierry Meinnel
Carmela Giglione

Résumé

N-(α)-terminal protein acetylation (NTA) is a widespread and essential protein modification. The reaction is catalyzed by various N-acetyltransferases (Nats) composed of a catalytic subunit alone or in complex with one or several factors. Their substrate specificities are largely determined by the first two N-terminal amino acids of the substrate protein. NTA is considered as an irreversible mark and mostly occurs co-translationally. A multiplicity of NTA roles have been uncovered such as its involvement in influencing protein's half-life. However, the majority of the proteome undergoes NTA with a high stoichiometry suggesting that NTA fulfils a broader and collective function, yet to be discovered. In this context, it has been suggested that NTA participates in maintaining protein homeostasis or proteostasis. The nucleus is rich in metastable and stress sensitive proteins suggesting that specific protein quality control strategies are in place to maintain nuclear proteostasis. Indeed
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Dates et versions

hal-03852104 , version 1 (14-11-2022)

Identifiants

  • HAL Id : hal-03852104 , version 1

Citer

Yuliya Kuchkovska, Jean-Baptiste Boyer, Thierry Meinnel, Carmela Giglione, Frédéric Frottin. N-terminal acetylation status of nuclear proteins upon proteotoxic stress. Protein termini: From mechanisms to biological impact, Jun 2022, Bergen, Norway. 2022. ⟨hal-03852104⟩
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