Open AccessEvidence for an unusual mechanism of membrane translocation of the periplasmic hydrogenase of Desulfovibrio vulgaris (Hildenborough), as derived from expression in Escherichia coli
Author(s) -
Dongen Walter,
Hagen Wilfred,
Berg Willy,
Veeger Cees
Publication year - 1988
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1988.tb02902.x
Subject(s) - periplasmic space , desulfovibrio vulgaris , escherichia coli , protein subunit , biology , hydrogenase , biochemistry , enzyme , bacterial outer membrane , cytoplasm , inner membrane , recombinant dna , microbiology and biotechnology , gene , bacteria , membrane , genetics
Using a subcellular fraction procedure, the location in the cell has been studied of the recombinant hydrogenase as expressed by an Escherichia coli clone carrying the structural genes for both the subunits of the Desulfovibrio vulgaris enzyme. In D. vulgaris the enzyme was extracted with the periplasmic fraction. However, when expressed in E. coli , only a minor portion of the recombinant enzyme co‐fractionated with the periplasm: the majority of the larger subunit was detected in the cytoplasmic fraction in E. coli , while most of the smaller subunit was found, in precursor form, in the membrane fraction. In E. coli clones in which the gene for either one of the subunits had been deleted, the export of the other subunit was completely abolished. These observations indicate that a special mechanism, which functions only poorly in E. coli , is involved in translocation of the enzyme across the inner membrane. Some factors of potential relevance for this poor transtranslocation; in E. coli are discussed.