Format

Send to

Choose Destination
Arch Microbiol. 1999 Oct;172(4):227-32.

The role of the twin-arginine motif in the signal peptide encoded by the hydA gene of the hydrogenase from wolinella succinogenes

Author information

1
Institut fur Mikrobiologie, Johann Wolfgang Goethe-Universitat, Marie-Curie-Strasse 9, D-60439 Frankfurt am Main, Germany.

Abstract

The hydABC operon of Wolinella succinogenes encodes the three subunits of the membrane-integrated Ni-hydrogenase. The catalytic subunit, HydB, is on the periplasmic side of the membrane. Residues R41 and R42 of the twin-arginine motif within the signal peptide of the precursor of the iron-sulfur subunit, HydA, were replaced by two glutamine residues. The corresponding mutant did not grow with H(2) as the electron donor of anaerobic respiration. Mature HydB and the precursor protein of HydA were located exclusively in the cytoplasmic cell fraction of the mutant, which catalyzed the reduction of benzyl viologen by H(2), suggesting that HydB contained Ni. The HydC protein was located in the membrane fraction of the mutant in wild-type amounts. HydC was purified and was shown to contain heme. The results suggest that HydA and HydB are translocated across the membrane by the Tat (twin-arginine translocation) system. The translocation of HydA and HydB as well as the maturation of the precursor protein of HydA appear to depend on the presence of the twin-arginine motif. In contrast, maturation of HydB, the insertion of HydC into the membrane, and heme attachment to HydC are apparently independent of the twin-arginine motif and do not require translocation of the two other hydrogenase subunits.

PMID:
10525739
DOI:
10.1007/s002030050764

Supplemental Content

Full text links

Icon for Springer
Loading ...
Support Center