Evidence map›Paper›PMID 18034796›Full record

ArticleMolecular microbiology2008

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

Lee Gyan Kwa, Dominik Wegmann, Britta Brügger, Felix T Wieland, Gerhard Wanner, Paula Braun

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 28% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Analyzing effects of naturally occurring missense mutations.Computational and mathematical methods in medicine · 2012
    Article
  7. Specificity of intramembrane protein-lipid interactions.Cold Spring Harbor perspectives in biology · 2011
    Review
  8. Article
  9. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Lee Gyan KwaDepartment Biologie I der LM-Universität München, Botanik, 80638 München, Germany.
Dominik Wegmann
Britta Brügger
Felix T Wieland
Gerhard Wanner
Paula Braun
Heidelberg University · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Mutation, MissenseAmino Acid SequenceBinding SitesCell MembraneGlutamatesLight-Harvesting Protein ComplexesMass SpectrometryMolecular StructureMutagenesis, Site-DirectedPhospholipidsProtein ConformationRhodobacter sphaeroidesSpectrophotometry, UltravioletGlutamatesLight-Harvesting Protein ComplexesPhospholipids

Identifiers

PMID18034796
PMCPMC2229836
OpenAlexW2109301107

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.