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Mutation of a single residue, β-glutamate-20, alters protein–lipid interactions of light harvesting complex II

It is well established that assembly of the peripheral antenna complex, LH2, is required for proper photosynthetic membrane biogenesis in the purple bacterium Rhodobacter sphaeroides. The underlying interactions are, as yet, not understood. Here we examined the relationship between the morphology of...

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Autores principales: Kwa, Lee Gyan, Wegmann, Dominik, Brügger, Britta, Wieland, Felix T, Wanner, Gerhard, Braun, Paula
Formato: Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2229836/
https://www.ncbi.nlm.nih.gov/pubmed/18034796
http://dx.doi.org/10.1111/j.1365-2958.2007.06017.x
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author Kwa, Lee Gyan
Wegmann, Dominik
Brügger, Britta
Wieland, Felix T
Wanner, Gerhard
Braun, Paula
author_facet Kwa, Lee Gyan
Wegmann, Dominik
Brügger, Britta
Wieland, Felix T
Wanner, Gerhard
Braun, Paula
author_sort Kwa, Lee Gyan
collection PubMed
description It is well established that assembly of the peripheral antenna complex, LH2, is required for proper photosynthetic membrane biogenesis in the purple bacterium Rhodobacter sphaeroides. The underlying interactions are, as yet, not understood. Here we examined the relationship between the morphology of the photosynthetic membrane and the lipid–protein interactions at the LH2–lipid interface. The non-bilayer lipid, phosphatidylethanolamine, is shown to be highly enriched in the boundary lipid phase of LH2. Sequence alignments indicate a putative lipid binding site, which includes β-glutamate-20 and the adjacent carotenoid end group. Replacement of β-glutamate-20 with alanine results in significant reduction of phosphatidylethanolamine and concomitant raise in phosphatidylcholine in the boundary lipid phase of LH2 without altering the lipid composition of the bulk phase. The morphology of the LH2 housing membrane is, however, unaffected by the amino acid replacement. In contrast, simultaneous modification of glutamate-20 and exchange of the carotenoid sphaeroidenone with neurosporene results in significant enlargement of the vesicular membrane invaginations. These findings suggest that the LH2 complex, specifically β-glutamate-20 and the carotenoids' polar head group, contribute to the shaping of the photosynthetic membrane by specific interactions with surrounding lipid molecules.
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spelling pubmed-22298362008-02-12 Mutation of a single residue, β-glutamate-20, alters protein–lipid interactions of light harvesting complex II Kwa, Lee Gyan Wegmann, Dominik Brügger, Britta Wieland, Felix T Wanner, Gerhard Braun, Paula Mol Microbiol Research Articles It is well established that assembly of the peripheral antenna complex, LH2, is required for proper photosynthetic membrane biogenesis in the purple bacterium Rhodobacter sphaeroides. The underlying interactions are, as yet, not understood. Here we examined the relationship between the morphology of the photosynthetic membrane and the lipid–protein interactions at the LH2–lipid interface. The non-bilayer lipid, phosphatidylethanolamine, is shown to be highly enriched in the boundary lipid phase of LH2. Sequence alignments indicate a putative lipid binding site, which includes β-glutamate-20 and the adjacent carotenoid end group. Replacement of β-glutamate-20 with alanine results in significant reduction of phosphatidylethanolamine and concomitant raise in phosphatidylcholine in the boundary lipid phase of LH2 without altering the lipid composition of the bulk phase. The morphology of the LH2 housing membrane is, however, unaffected by the amino acid replacement. In contrast, simultaneous modification of glutamate-20 and exchange of the carotenoid sphaeroidenone with neurosporene results in significant enlargement of the vesicular membrane invaginations. These findings suggest that the LH2 complex, specifically β-glutamate-20 and the carotenoids' polar head group, contribute to the shaping of the photosynthetic membrane by specific interactions with surrounding lipid molecules. Blackwell Publishing Ltd 2008-01 2007-11-22 /pmc/articles/PMC2229836/ /pubmed/18034796 http://dx.doi.org/10.1111/j.1365-2958.2007.06017.x Text en © 2007 The Authors Journal compilation © 2007 Blackwell Publishing Ltd https://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.
spellingShingle Research Articles
Kwa, Lee Gyan
Wegmann, Dominik
Brügger, Britta
Wieland, Felix T
Wanner, Gerhard
Braun, Paula
Mutation of a single residue, β-glutamate-20, alters protein–lipid interactions of light harvesting complex II
title Mutation of a single residue, β-glutamate-20, alters protein–lipid interactions of light harvesting complex II
title_full Mutation of a single residue, β-glutamate-20, alters protein–lipid interactions of light harvesting complex II
title_fullStr Mutation of a single residue, β-glutamate-20, alters protein–lipid interactions of light harvesting complex II
title_full_unstemmed Mutation of a single residue, β-glutamate-20, alters protein–lipid interactions of light harvesting complex II
title_short Mutation of a single residue, β-glutamate-20, alters protein–lipid interactions of light harvesting complex II
title_sort mutation of a single residue, β-glutamate-20, alters protein–lipid interactions of light harvesting complex ii
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2229836/
https://www.ncbi.nlm.nih.gov/pubmed/18034796
http://dx.doi.org/10.1111/j.1365-2958.2007.06017.x
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