Monitoring pyrene excimers in lactose permease liposomes: Revealing the presence of phosphatidylglycerol in proximity to an integral membrane protein

Laura Picas, Sandra Merino-Montero, Antoni Morros, Jordi Hernández-Borrell, M. Teresa Montero

Research output: Contribution to journalArticleResearchpeer-review

5 Citations (Scopus)

Abstract

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. © 2006 Springer Science+Business Media, Inc.
Original languageEnglish
Pages (from-to)649-654
JournalJournal of Fluorescence
Volume17
Issue number6
DOIs
Publication statusPublished - 1 Nov 2007

Keywords

  • Energy transfer
  • Lactose permease
  • Proteoliposomes
  • Pyrene excimer formation
  • Tryptophan

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