Proteomics

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Proteomic analysis of the reaction center-light harvesting 1 complex from Rhodobacter sphaeroides, identifying a previously uncharacterized protein component encoded by a newly-identified ORF.

ABSTRACT: Photosynthesis in purple bacteria, represented by Rhodobacter sphaeroides as a long-established model organism, utilizes a protein-cofactor complex to capture solar energy. This complex is embedded in specialized spherical membrane structures and comprises a central reaction center (RC) encircled by a ring of light harvesting 1 (LH1) polypeptides. An additional protein PufX has two functions: (1) facilitating ubiquinone/ubiquinol exchange between the RC and membrane and (2) inducing complex dimerization – important for maintaining the curvature of the membrane structures. Cryo-EM has revealed a further component that facilitates dimerization, with proteomic analysis confirming its identity as a previously uncharacterized protein encoded by a newly-identified ORF.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Rhodobacter Sphaeroides 2.4.1

SUBMITTER: Philip Jackson  

LAB HEAD: Christopher Neil Hunter

PROVIDER: PXD028553 | Pride | 2022-02-16

REPOSITORIES: Pride

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Publications

Cryo-EM structure of the dimeric Rhodobacter sphaeroides RC-LH1 core complex at 2.9 Å: the structural basis for dimerisation.

Qian Pu P   Croll Tristan I TI   Hitchcock Andrew A   Jackson Philip J PJ   Salisbury Jack H JH   Castro-Hartmann Pablo P   Sader Kasim K   Swainsbury David J K DJK   Hunter C Neil CN  

The Biochemical journal 20211101 21

The dimeric reaction centre light-harvesting 1 (RC-LH1) core complex of Rhodobacter sphaeroides converts absorbed light energy to a charge separation, and then it reduces a quinone electron and proton acceptor to a quinol. The angle between the two monomers imposes a bent configuration on the dimer complex, which exerts a major influence on the curvature of the membrane vesicles, known as chromatophores, where the light-driven photosynthetic reactions take place. To investigate the dimerisation  ...[more]

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