Growth substrate dependent localization of tetrachloroethene reductive dehalogenase in Sulfurospirillum multivorans.
Sulfurospirillum multivorans is a dehalorespiring organism, which is able to utilize tetrachloroethene as terminal electron acceptor in an anaerobic respiratory chain. The localization of the tetrachloroethene reductive dehalogenase in dependence on different growth substrates was studied using the freeze-fracture replica immunogold labeling technique. When the cells were grown with pyruvate plus fumarate, a major part of the enzyme was either localized in the cytoplasm or membrane associated facing the cytoplasm. In cells grown on pyruvate or formate as electron donors and tetrachloroethene as electron acceptor, most of the enzyme was detected at the periplasmic side of the cytoplasmic membrane. These results were confirmed by immunoblots of the enzyme with and without the twin arginine leader peptide. Trichloroethene exhibited the same effect on the enzyme localization as tetrachloroethene. The data indicated that the localization of the enzyme was dependent on the electron acceptor utilized.
John
Markus
M
Institute for Microbiology, Friedrich-Schiller-University, Philosophenweg 12, 07743 Jena, Germany.
Schmitz
Roland P H
RP
Westermann
Martin
M
Richter
Walter
W
Diekert
Gabriele
G
D001426:Bacterial Proteins / Q000032:analysis; D002462:Cell Membrane / Q000201:enzymology; D003593:Cytoplasm / Q000201:enzymology; D020565:Epsilonproteobacteria / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D005561:Formates / Q000378:metabolism; D005650:Fumarates / Q000378:metabolism; D015151:Immunoblotting; D016253:Microscopy, Immunoelectron / Q000379:methods; D008954:Models, Biological; D010088:Oxidoreductases / Q000032:analysis*; D019289:Pyruvic Acid / Q000378:metabolism
D001426:Bacterial Proteins; D005561:Formates; D005650:Fumarates; C030544:formic acid; D019289:Pyruvic Acid; D010088:Oxidoreductases; C112990:tetrachloroethene dehalogenase