Monitoring Pyrene Excimers in Lactose Permease Liposomes: Revealing the Presence of Phosphatidylglycerol in Proximity to an Integral Membrane Protein - Institut Curie Accéder directement au contenu
Article Dans Une Revue Journal of Fluorescence Année : 2007

Monitoring Pyrene Excimers in Lactose Permease Liposomes: Revealing the Presence of Phosphatidylglycerol in Proximity to an Integral Membrane Protein

Laura Picas
Sandra Merino-Montero
  • Fonction : Auteur
Antoni Morros
  • Fonction : Auteur
Jordi Hernández-Borrell
  • Fonction : Auteur
M Teresa Montero
  • Fonction : Auteur
M. Teresa Montero
  • Fonction : Auteur

Résumé

In this study, we examined the annular lipid composition of the transmembrane protein lactose permease (LacY) from Escherichia coli. LacY was reconstituted into 1-Palmitoyl-2-Oleoyl-sn-Glycero-3-Phosphoethanolamine (POPE) and 1-Palmitoyl-2-Oleoyl-sn-Glycero-3-3-[Phospho-rac-(1-glycerol)] (POPG) and labeled with 1-hexadecanoyl-2-(1-pyrenedecanoyl)-sn-Glycero-3-phosphoglycerol (PPDPG) at a 3:0.99:0.01 molar ratio. Pyrene excimer formation was monitored by exciting a single tryptophan mutant of the protein (T320W). The results suggest that POPG remains segregated in the vicinity of the protein, most likely forming part of the annular composition. The possible involvement of POPG in hydrogen binding with the protein, as well as the molecular mechanism of LacY, is also discussed in the context of the proteomic network theory.

Domaines

Biophysique

Dates et versions

hal-02289066 , version 1 (16-09-2019)

Identifiants

Citer

Laura Picas, Sandra Merino-Montero, Antoni Morros, Jordi Hernández-Borrell, M Teresa Montero, et al.. Monitoring Pyrene Excimers in Lactose Permease Liposomes: Revealing the Presence of Phosphatidylglycerol in Proximity to an Integral Membrane Protein. Journal of Fluorescence, 2007, 17 (6), pp.649-654. ⟨10.1007/s10895-006-0073-0⟩. ⟨hal-02289066⟩
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