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Incorporation of chlorophyll a into Rhodobacter sphaeroides

ABSTRACT: Heterologous expression of a water soluble chlorophyll protein from Brassica oleracea var. gemmifera in the phototrophic purple bacterium Rhodobacter sphaeroides was verified by bottom-up proteomic analysis.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Brassica Oleracea Var. Gemmifera (brussel Sprouts)

TISSUE(S): Photosynthetic Cell

SUBMITTER: Philip Jackson

LAB HEAD: Mark Dickman

PROVIDER: PXD002638 | Pride | 2016-07-12

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20150724_PJ_wscp_1_50.mgf	Mgf
	20150724_PJ_wscp_1_50.raw	Raw
	F031401.dat	Other
	F031401.dat-pride.pride.mgf.gz	Mgf
	F031401.dat-pride.pride.mztab.gz	Mztab

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Publications

Biosynthesis of Chlorophyll a in a Purple Bacterial Phototroph and Assembly into a Plant Chlorophyll-Protein Complex.

Hitchcock Andrew A Jackson Philip J PJ Chidgey Jack W JW Dickman Mark J MJ Hunter C Neil CN Canniffe Daniel P DP

ACS synthetic biology 20160524 9

Improvements to photosynthetic efficiency could be achieved by manipulating pigment biosynthetic pathways of photosynthetic organisms in order to increase the spectral coverage for light absorption. The development of organisms that can produce both bacteriochlorophylls and chlorophylls is one way to achieve this aim, and accordingly we have engineered the bacteriochlorophyll-utilizing anoxygenic phototroph Rhodobacter sphaeroides to make chlorophyll a. Bacteriochlorophyll and chlorophyll share ...[more]

PMID: 27171912

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Confirmation of the subunit composition of Rhodobacter sphaeroides cytochrome bc1 complex isolated in styrene maleic acid nanodiscs.

Project description:The purple α-proteobacterium Rhodobacter sphaeroides is a long-established model organism owing to its ability to switch between aerobic, anaerobic and phototrophic metabolism. This organism is also of great interest because of its phylogenetic relationship with the bacterial progenitor of the mitochondrion in eukaryotes. A component of the electron transport chain in both bacteria and mitochondria is the cytochrome bc1 (cytbc1) complex, a quinol:cytochrome c oxidoreductase that translocates protons across energy-transducing membranes. The resulting proton motive force is then utilized to drive ATP synthesis. Cytbc1 comprises three core subunits together with, in some organisms, one or more additional subunits. In Rhodobacter sphaeroides, the one additional subunit (subunit IV) is not fully characterized in terms of both structure and function. In this project, proteomic analysis is used to confirm the presence of all four subunits in a cytbc1 preparation isolated in SMA nanodiscs for structural analysis by cryo-EM.

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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.

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Structural characterization of the reaction center-light harvesting 1-PufXY complex from Rhodobacter sphaeroides

Project description: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. The energy derived from light absorption drives the reduction of ubiquinone, entering from the membrane, to generate ubiquinol. The photosynthetic cycle is therefore dependent on the exchange of ubiquinone and ubiquinol to and from the RC. This exchange requires an additional protein (PufX) which prevents complete closure of the LH1 ring, leaving a channel which connects the RC with the membrane. The structure of the RC-LH1-PufX complex is under investigation by cryo-EM, revealing the presence of a previously undiscovered protein (PufY) that is also involved in channel formation. Proteomic analysis has verified the identities of the expected protein components of this complex, additionally confirming the presence of the newly-discovered PufY polypeptide mapped into the cryo-EM structure.

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Expression data from H2-producing Rhodobacter sphaeroides cultures fed different organic substrates

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RpoHI and RpoHII regulons in Rhodobacter sphaeroides 2.4.1 from gene expression profiling

Project description:In this study, we performed expression profiling experiments to determine the respective regulons of RpoHI and RpoHII in Rhodobacter sphaeroides. We grew R. sphaeroides in aerobic conditions and induced either proteins ectopically and compared the global gene expression profiles. The expression profiles of R. sphaeroides strains lacking either RpoHI or RpoHII were compered to strains expressing RpoHI or RpoHII ectopically from a plasmid to detect gene differentially expressed. Three biological replicates were performed for each strain.

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PpsR regulon in Rhodobacter sphaeroides

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Expression Profile of R. capsulatus under heat and cold stress

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