Mutation of a single residue, beta-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 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 beta-glutamate-20 and the adjacent carotenoid end group. Replacement of beta-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 beta-glutamate-20 and the carotenoids' polar head group, contribute to the shaping of the photosynthetic membrane by specific interactions with surrounding lipid molecules.
Department Biologie I der LM-Universität München, Botanik, 80638 München, Germany.
Lee Gyan
LG
Kwa
Dominik
D
Wegmann
Britta
B
Brügger
Felix T
FT
Wieland
Gerhard
G
Wanner
Paula
P
Braun
D000595:Amino Acid Sequence; D001665:Binding Sites; D002462:Cell Membrane / Q000737:chemistry*; D005971:Glutamates / Q000235:genetics / Q000378:metabolism*; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry* / Q000235:genetics*; D013058:Mass Spectrometry; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D020125:Mutation, Missense; D010743:Phospholipids / Q000378:metabolism*; D011487:Protein Conformation; D012242:Rhodobacter sphaeroides / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D013056:Spectrophotometry, Ultraviolet
D005971:Glutamates; D045342:Light-Harvesting Protein Complexes; D010743:Phospholipids