ArticleThe Journal of biological chemistry2014
Aberrant assembly complexes of the reaction center light-harvesting 1 PufX (RC-LH1-PufX) core complex of Rhodobacter sphaeroides imaged by atomic force microscopy.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Integration of transcriptomics and metabolomics for understanding the global responses to neutral pH and high pH under high light in photosynthetic bacteriumApplied and environmental microbiology · 2025Article
- Excitation energy transfer in proteoliposomes reconstituted with LH2 and RC-LH1 complexes from Rhodobacter sphaeroides.Bioscience reports · 2024Article
- The structure and assembly of reaction centre-light-harvesting 1 complexes in photosynthetic bacteria.Bioscience reports · 2023Article
- Structural basis for the assembly and quinone transport mechanisms of the dimeric photosynthetic RC-LH1 supercomplex.Nature communications · 2022Article
- Cryo-EM structure of the dimeric Rhodobacter sphaeroides RC-LH1 core complex at 2.9 Å: the structural basis for dimerisation.The Biochemical journal · 2021Article
- Cryo-EM structure of the monomeric Rhodobacter sphaeroides RC-LH1 core complex at 2.5 Å.The Biochemical journal · 2021Article
- Cryo-EM structure of the Rhodospirillum rubrum RC-LH1 complex at 2.5 Å.The Biochemical journal · 2021Article
- Identification of protein W, the elusive sixth subunit of the Rhodopseudomonas palustris reaction center-light harvesting 1 core complex.Biochimica et biophysica acta. Bioenergetics · 2018Article
- Mapping the ultrafast flow of harvested solar energy in living photosynthetic cells.Nature communications · 2017Article
- The C-terminus of PufX plays a key role in dimerisation and assembly of the reaction center light-harvesting 1 complex from Rhodobacter sphaeroides.Biochimica et biophysica acta. Bioenergetics · 2017Article
- The PufX quinone channel enables the light-harvesting 1 antenna to bind more carotenoids for light collection and photoprotection.FEBS letters · 2017Article
- Electronic Structure and Dynamics of Higher-Lying Excited States in Light Harvesting Complex 1 from Rhodobacter sphaeroides.The journal of physical chemistry. A · 2016Article
- PucC and LhaA direct efficient assembly of the light-harvesting complexes in Rhodobacter sphaeroides.Molecular microbiology · 2016Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
In the purple phototrophic bacterium Rhodobacter sphaeroides, many protein complexes congregate within the membrane to form operational photosynthetic units consisting of arrays of light-harvesting LH2 complexes and monomeric and dimeric reaction center (RC)-light-harvesting 1 (LH1)-PufX "core" complexes. Each half of a dimer complex consists of a RC surrounded by 14 LH1 αβ subunits, with two bacteriochlorophylls (Bchls) sandwiched between each αβ pair of transmembrane helices. We used atomic force microscopy (AFM) to investigate the assembly of single molecules of the RC-LH1-PufX complex using membranes prepared from LH2-minus mutants. When the RC and PufX components were also absent, AFM revealed a series of LH1 variants where the repeating α(1)β(1)(Bchl)2 units had formed rings of variable size, ellipses, and spirals and also arcs that could be assembly products. The spiral complexes occur when the LH1 ring has failed to close, and short arcs are suggestive of prematurely terminated LH1 complex assembly. In the absence of RCs, we occasionally observed captive proteins enclosed by the LH1 ring. When production of LH1 units was restricted by lowering the relative levels of the cognate pufBA transcript, we imaged a mixture of complete RC-LH1 core complexes, empty LH1 rings, and isolated RCs, leading us to conclude that once a RC associates with the first α1β1(Bchl)2 subunit, cooperative associations between subsequent subunits and the RC tend to drive LH1 ring assembly to completion.
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