The light-harvesting antenna of Chlorobium tepidum: interactions between the FMO protein and the major chlorosome protein CsmA studied by surface plasmon resonance.
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.
Pedersen
Marie Østergaard
MØ
Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK5230, Odense M, Denmark.
Borch
Jonas
J
Højrup
Peter
P
Cox
Raymond P
RP
Miller
Mette
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D041883:Chlorobium / Q000378:metabolism*; D045342:Light-Harvesting Protein Complexes / Q000378:metabolism*; D013045:Species Specificity; D020349:Surface Plasmon Resonance
D001426:Bacterial Proteins; C404706:CsmA protein, Chlorobium tepidum; C086320:FMO bacteriochlorophyll protein, Bacteria; D045342:Light-Harvesting Protein Complexes