| Autor: |
Saer RG; Department of Biology, Washington University in St. Louis, 1 Brookings Drive, St. Louis, MO, 63130, USA.; Photosynthetic Antenna Research Center (PARC), Washington University in St. Louis, 1 Brookings Drive, St. Louis, MO, 63130, USA., Schultz RL; Department of Chemistry, Washington University in St. Louis, 1 Brookings Drive, St. Louis, MO, 63130, USA.; Department of Chemistry, University of Wisconsin Madison, Madison, WI, 53706, USA., Blankenship RE; Department of Biology, Washington University in St. Louis, 1 Brookings Drive, St. Louis, MO, 63130, USA. blankenship@wustl.edu.; Department of Chemistry, Washington University in St. Louis, 1 Brookings Drive, St. Louis, MO, 63130, USA. blankenship@wustl.edu. |
| Abstrakt: |
The trimeric nature of the Fenna-Matthews-Olson (FMO) protein antenna complex from green sulfur phototrophic bacteria was investigated. Mutations were introduced into the protein at positions 142 and 198, which were chosen to destabilize the intra-trimer salt bridges between adjacent monomers. Strains bearing the mutations R142L, R198L, or their combination, exhibited altered optical absorption spectra of purified membranes and fluoresced more intensely than the wild type. In particular, the introduction of the R142L mutation resulted in slower culture growth rates, as well as an FMO complex that was not able to be isolated in appreciable quantities, while the R198L mutation yielded an FMO complex with increased sensitivity to sodium thiocyanate and Triton X-100 treatments. Native and denaturing PAGE experiments suggest that much of the FMO complexes in the mutant strains pool with the insoluble material upon membrane solubilization with n-dodecyl β-D-maltoside, a mild nonionic detergent. Taken together, our results suggest that the quaternary structure of the FMO complex, the homotrimer, is an important factor in the maintenance of the complex's tertiary structure. |
Full text from SpringerLink