Shotgun proteomic analysis of a chromatophore-enriched preparation from the purple phototrophic bacterium Rhodopseudomonas palustris View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-12

AUTHORS

Anthony P. Fejes, Eugene C. Yi, David R. Goodlett, J. Thomas Beatty

ABSTRACT

A proteomics approach was evaluated for analysis of photosyntheis-related proteins that are characteristic of chromatophores, particles derived from purple phototrophic bacterial intracytoplasmic membranes. Proteins of purified chromatophores from Rhodopseudomonas palustris were solubilized and digested with trypsin, to create a collection of peptides that were fractionated by liquid chromatography. Peptide sequences were determined and assigned to specific proteins by analysis of tandem mass spectra of peptides, and comparison to a library derived from the recently determined R. palustris genome sequence. A total of 300 proteins were detected with a probability value ≥0.9, and the number of proteins detected increased to 345 when the minimum probability value was reduced to 0.5. Membrane–integral proteins of the reaction center, cytochrome b/c1, light-harvesting and ATPase complexes were used as controls to assess how well this approach performs with hydrophobic proteins. New genes were identified, and tentatively designated as encoding photosynthesis-related proteins. We conclude that this approach is a powerful method to evaluate the possible existence of new photosynthesis-related proteins (and genes), although alternative methods are needed to evaluate the exact functions of newly discovered genes. More... »

PAGES

195-203

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/b:pres.0000006752.81486.74

DOI

http://dx.doi.org/10.1023/b:pres.0000006752.81486.74

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1021746993

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16245051


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