Structure and stability of the spinach aquaporin SoPIP2;1 in detergent micelles and lipid membranes

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Structure and stability of the spinach aquaporin SoPIP2;1 in detergent micelles and lipid membranes. / Plasencia, Inés; Survery, Sabeen; Ibragimova, Sania; Hansen, Jesper S.; Kjellbom, Per; Helix-Nielsen, Claus; Johanson, Urban; Mouritsen, Ole G.

In: PLoS ONE, Vol. 6, No. 2, e14674, 28.02.2011.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Plasencia, I, Survery, S, Ibragimova, S, Hansen, JS, Kjellbom, P, Helix-Nielsen, C, Johanson, U & Mouritsen, OG 2011, 'Structure and stability of the spinach aquaporin SoPIP2;1 in detergent micelles and lipid membranes', PLoS ONE, vol. 6, no. 2, e14674. https://doi.org/10.1371/journal.pone.0014674

APA

Plasencia, I., Survery, S., Ibragimova, S., Hansen, J. S., Kjellbom, P., Helix-Nielsen, C., Johanson, U., & Mouritsen, O. G. (2011). Structure and stability of the spinach aquaporin SoPIP2;1 in detergent micelles and lipid membranes. PLoS ONE, 6(2), [e14674]. https://doi.org/10.1371/journal.pone.0014674

Vancouver

Plasencia I, Survery S, Ibragimova S, Hansen JS, Kjellbom P, Helix-Nielsen C et al. Structure and stability of the spinach aquaporin SoPIP2;1 in detergent micelles and lipid membranes. PLoS ONE. 2011 Feb 28;6(2). e14674. https://doi.org/10.1371/journal.pone.0014674

Author

Plasencia, Inés ; Survery, Sabeen ; Ibragimova, Sania ; Hansen, Jesper S. ; Kjellbom, Per ; Helix-Nielsen, Claus ; Johanson, Urban ; Mouritsen, Ole G. / Structure and stability of the spinach aquaporin SoPIP2;1 in detergent micelles and lipid membranes. In: PLoS ONE. 2011 ; Vol. 6, No. 2.

Bibtex

@article{b8e5e3bae5954cd58e50b547da46504b,
title = "Structure and stability of the spinach aquaporin SoPIP2;1 in detergent micelles and lipid membranes",
abstract = "Background: SoPIP2;1 constitutes one of the major integral proteins in spinach leaf plasma membranes and belongs to the aquaporin family. SoPIP2;1 is a highly permeable and selective water channel that has been successfully overexpressed and purified with high yields. In order to optimize reconstitution of the purified protein into biomimetic systems, we have here for the first time characterized the structural stability of SoPIP2;1. Methodology/Principal Finding: We have characterized the protein structural stability after purification and after reconstitution into detergent micelles and proteoliposomes using circular dichroism and fluorescence spectroscopy techniques. The structure of SoPIP2;1 was analyzed either with the protein solubilized with octyl-β-D-glucopyranoside (OG) or reconstituted into lipid membranes formed by E. coli lipids, diphytanoylphosphatidylcholine (DPhPC), or reconstituted into lipid membranes formed from mixtures of 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPE), 1-palmitoyl-2oleoyl-phosphatidylethanolamine (POPE), 1-palmitoyl-2-oleoyl-phosphatidylserine (POPS), and ergosterol. Generally, SoPIP2;1 secondary structure was found to be predominantly α-helical in accordance with crystallographic data. The protein has a high thermal structural stability in detergent solutions, with an irreversible thermal unfolding occurring at a melting temperature of 58°C. Incorporation of the protein into lipid membranes increases the structural stability as evidenced by an increased melting temperature of up to 70°C. Conclusion/Significance: The results of this study provide insights into SoPIP2;1 stability in various host membranes and suggest suitable choices of detergent and lipid composition for reconstitution of SoPIP2;1 into biomimetic membranes for biotechnological applications.",
author = "In{\'e}s Plasencia and Sabeen Survery and Sania Ibragimova and Hansen, {Jesper S.} and Per Kjellbom and Claus Helix-Nielsen and Urban Johanson and Mouritsen, {Ole G.}",
year = "2011",
month = feb,
day = "28",
doi = "10.1371/journal.pone.0014674",
language = "English",
volume = "6",
journal = "P L o S One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "2",

}

RIS

TY - JOUR

T1 - Structure and stability of the spinach aquaporin SoPIP2;1 in detergent micelles and lipid membranes

AU - Plasencia, Inés

AU - Survery, Sabeen

AU - Ibragimova, Sania

AU - Hansen, Jesper S.

AU - Kjellbom, Per

AU - Helix-Nielsen, Claus

AU - Johanson, Urban

AU - Mouritsen, Ole G.

PY - 2011/2/28

Y1 - 2011/2/28

N2 - Background: SoPIP2;1 constitutes one of the major integral proteins in spinach leaf plasma membranes and belongs to the aquaporin family. SoPIP2;1 is a highly permeable and selective water channel that has been successfully overexpressed and purified with high yields. In order to optimize reconstitution of the purified protein into biomimetic systems, we have here for the first time characterized the structural stability of SoPIP2;1. Methodology/Principal Finding: We have characterized the protein structural stability after purification and after reconstitution into detergent micelles and proteoliposomes using circular dichroism and fluorescence spectroscopy techniques. The structure of SoPIP2;1 was analyzed either with the protein solubilized with octyl-β-D-glucopyranoside (OG) or reconstituted into lipid membranes formed by E. coli lipids, diphytanoylphosphatidylcholine (DPhPC), or reconstituted into lipid membranes formed from mixtures of 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPE), 1-palmitoyl-2oleoyl-phosphatidylethanolamine (POPE), 1-palmitoyl-2-oleoyl-phosphatidylserine (POPS), and ergosterol. Generally, SoPIP2;1 secondary structure was found to be predominantly α-helical in accordance with crystallographic data. The protein has a high thermal structural stability in detergent solutions, with an irreversible thermal unfolding occurring at a melting temperature of 58°C. Incorporation of the protein into lipid membranes increases the structural stability as evidenced by an increased melting temperature of up to 70°C. Conclusion/Significance: The results of this study provide insights into SoPIP2;1 stability in various host membranes and suggest suitable choices of detergent and lipid composition for reconstitution of SoPIP2;1 into biomimetic membranes for biotechnological applications.

AB - Background: SoPIP2;1 constitutes one of the major integral proteins in spinach leaf plasma membranes and belongs to the aquaporin family. SoPIP2;1 is a highly permeable and selective water channel that has been successfully overexpressed and purified with high yields. In order to optimize reconstitution of the purified protein into biomimetic systems, we have here for the first time characterized the structural stability of SoPIP2;1. Methodology/Principal Finding: We have characterized the protein structural stability after purification and after reconstitution into detergent micelles and proteoliposomes using circular dichroism and fluorescence spectroscopy techniques. The structure of SoPIP2;1 was analyzed either with the protein solubilized with octyl-β-D-glucopyranoside (OG) or reconstituted into lipid membranes formed by E. coli lipids, diphytanoylphosphatidylcholine (DPhPC), or reconstituted into lipid membranes formed from mixtures of 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPE), 1-palmitoyl-2oleoyl-phosphatidylethanolamine (POPE), 1-palmitoyl-2-oleoyl-phosphatidylserine (POPS), and ergosterol. Generally, SoPIP2;1 secondary structure was found to be predominantly α-helical in accordance with crystallographic data. The protein has a high thermal structural stability in detergent solutions, with an irreversible thermal unfolding occurring at a melting temperature of 58°C. Incorporation of the protein into lipid membranes increases the structural stability as evidenced by an increased melting temperature of up to 70°C. Conclusion/Significance: The results of this study provide insights into SoPIP2;1 stability in various host membranes and suggest suitable choices of detergent and lipid composition for reconstitution of SoPIP2;1 into biomimetic membranes for biotechnological applications.

UR - http://www.scopus.com/inward/record.url?scp=79951926849&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0014674

DO - 10.1371/journal.pone.0014674

M3 - Journal article

C2 - 21339815

AN - SCOPUS:79951926849

VL - 6

JO - P L o S One

JF - P L o S One

SN - 1932-6203

IS - 2

M1 - e14674

ER -

ID: 230975870