Source:http://linkedlifedata.com/resource/pubmed/id/16622783
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2006-6-8
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pubmed:abstractText |
The photosynthetic apparatus of purple bacteria in the genus Rhodobacter includes a core complex consisting of the reaction centre (RC), light-harvesting complex 1 (LH1), and the PufX protein. PufX modulates LH1 structure and facilitates photosynthetic quinone/quinol exchange. We deleted RC/LH1 genes in pufX+ and pufX++ (merodiploid) strains of Rhodobacter capsulatus, which reduced PufX levels regardless of pufX gene copy number and location. Photosynthetic growth of RC-only strains and independent assembly kinetics of the RC and LH1 were unaffected by pufX merodiploidy, but the absorption spectra of strains expressing the RC plus either LH1 alpha or beta indicated that PufX may influence bacteriochlorophyll binding environments. Significant self-association of the PufX transmembrane segment was detected in a hybrid protein expression system, consistent with a role of PufX in core complex dimerization, as proposed for other Rhodobacter species. Our results indicate that in R. capsulatus PufX has the potential to be a central, homodimeric core complex component, and its cellular level is increased by interactions with the RC and LH1.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Light-Harvesting Protein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Photosynthetic Reaction Center...,
http://linkedlifedata.com/resource/pubmed/chemical/PufX protein, Rhodobacter
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0166-8595
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
159-71
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pubmed:meshHeading |
pubmed-meshheading:16622783-Bacterial Proteins,
pubmed-meshheading:16622783-Gene Expression Regulation, Bacterial,
pubmed-meshheading:16622783-Light-Harvesting Protein Complexes,
pubmed-meshheading:16622783-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:16622783-Ploidies,
pubmed-meshheading:16622783-Rhodobacter capsulatus
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pubmed:year |
2006
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pubmed:articleTitle |
Investigation of Rhodobacter capsulatus PufX interactions in the core complex of the photosynthetic apparatus.
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pubmed:affiliation |
Department of Microbiology and Immunology, University of British Columbia, V6T 1Z3, Vancouver, BC, Canada. muktak@microbio.umass.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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