Abstract
Green sulfur bacteria possess two external light-harvesting antenna systems, the chlorosome and the FMO protein, which participate in a sequential energy transfer to the reaction centers embedded in the cytoplasmic membrane. However, little is known about the physical interaction between these two antenna systems. We have studied the interaction between the major chlorosome protein, CsmA, and the FMO protein in Chlorobium tepidum using surface plasmon resonance (SPR). Our results show an interaction between the FMO protein and an immobilized synthetic peptide corresponding to 17 amino acids at the C terminal of CsmA. This interaction is dependent on the presence of a motif comprising six amino acids that are highly conserved in all the currently available CsmA protein sequences.
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Abbreviations
- BChl:
-
Bacteriochlorophyll
- EDTA:
-
Ethylenediamine-tetraacetic acid
- FMO:
-
Fenna–Matthews–Olson
- MALDI-TOF MS:
-
Matrix-assisted laser desorption ionization time of flight mass spectrometry
- SDS:
-
Sodium dodecyl sulfate
- SPR:
-
Surface plasmon resonance
- TFA:
-
Trifluoroacetic acid
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This work was supported by a grant from the Danish Natural Science Research Council.
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Pedersen, M.Ø., Borch, J., Højrup, P. et al. The light-harvesting antenna of Chlorobium tepidum: Interactions between the FMO protein and the major chlorosome protein CsmA studied by surface plasmon resonance. Photosynth Res 89, 63–69 (2006). https://doi.org/10.1007/s11120-006-9081-9
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DOI: https://doi.org/10.1007/s11120-006-9081-9