Fiche publication
Date publication
novembre 2023
Journal
Scientific reports
Auteurs
Membres identifiés du Cancéropôle Est :
Dr DELARUE Patrice
,
Pr SENET Patrick
Tous les auteurs :
Bellanger T, da Silva Barreira D, Wien F, Delarue P, Senet P, Rieu A, Neiers F, Varela PF, Combet S, Weidmann S
Lien Pubmed
Résumé
To cope with environmental stresses, bacteria have developed different strategies, including the production of small heat shock proteins (sHSP). All sHSPs are described for their role as molecular chaperones. Some of them, like the Lo18 protein synthesized by Oenococcus oeni, also have the particularity of acting as a lipochaperon to maintain membrane fluidity in its optimal state following cellular stresses. Lipochaperon activity is poorly characterized and very little information is available on the domains or amino-acids key to this activity. The aim in this paper is to investigate the importance at the protein structure and function level of four highly conserved residues in sHSP exhibiting lipochaperon activity. Thus, by combining in silico, in vitro and in vivo approaches the importance of three amino-acids present in the core of the protein was shown to maintain both the structure of Lo18 and its functions.
Mots clés
Amino Acids, Heat-Shock Proteins, Small, metabolism, Molecular Chaperones, metabolism, Membrane Fluidity
Référence
Sci Rep. 2023 11 3;13(1):19036
