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

doi:10.1007/s10895-006-0073-0

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

Department of Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › Research › peer-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 language	English
Pages (from-to)	649-654
Journal	Journal of Fluorescence
Volume	17
Issue number	6
DOIs	https://doi.org/10.1007/s10895-006-0073-0
Publication status	Published - 1 Nov 2007

Keywords

Energy transfer
Lactose permease
Proteoliposomes
Pyrene excimer formation
Tryptophan

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

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. {\textcopyright} 2006 Springer Science+Business Media, Inc.",

keywords = "Energy transfer, Lactose permease, Proteoliposomes, Pyrene excimer formation, Tryptophan",

author = "Laura Picas and Sandra Merino-Montero and Antoni Morros and Jordi Hern{\'a}ndez-Borrell and Montero, {M. Teresa}",

year = "2007",

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doi = "10.1007/s10895-006-0073-0",

language = "English",

volume = "17",

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journal = "Journal of Fluorescence",

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Monitoring pyrene excimers in lactose permease liposomes: Revealing the presence of phosphatidylglycerol in proximity to an integral membrane protein. / Picas, Laura; Merino-Montero, Sandra; Morros, Antoni; Hernández-Borrell, Jordi; Montero, M. Teresa.

In: Journal of Fluorescence, Vol. 17, No. 6, 01.11.2007, p. 649-654.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - Monitoring pyrene excimers in lactose permease liposomes: Revealing the presence of phosphatidylglycerol in proximity to an integral membrane protein

AU - Picas, Laura

AU - Merino-Montero, Sandra

AU - Morros, Antoni

AU - Hernández-Borrell, Jordi

AU - Montero, M. Teresa

PY - 2007/11/1

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N2 - 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.

AB - 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.

KW - Energy transfer

KW - Lactose permease

KW - Proteoliposomes

KW - Pyrene excimer formation

KW - Tryptophan

U2 - 10.1007/s10895-006-0073-0

DO - 10.1007/s10895-006-0073-0

M3 - Article

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SP - 649

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JO - Journal of Fluorescence

JF - Journal of Fluorescence

SN - 1053-0509

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ER -