Affiliation:
1. Lehrstuhl für Technische Mikrobiologie, Fachbereich Chemietechnik, Universität Dortmund, D-44221 Dortmund, Germany
Abstract
ABSTRACT
The novel genes
soxFGH
were identified, completing the
sox
gene cluster of
Paracoccus pantotrophus
coding for enzymes involved in lithotrophic sulfur oxidation. The periplasmic SoxF, SoxG, and SoxH proteins were induced by thiosulfate and purified to homogeneity from the soluble fraction.
soxF
coded for a protein of 420 amino acids with a signal peptide containing a twin-arginine motif. SoxF was 37% identical to the flavoprotein FccB of flavocytochrome
c
sulfide dehydrogenase of
Allochromatium vinosum
. The mature SoxF (42,832 Da) contained 0.74 mol of flavin adenine dinucleotide per mol.
soxG
coded for a novel protein of 303 amino acids with a signal peptide containing a twin-arginine motif. The mature SoxG (29,657 Da) contained two zinc binding motifs and 0.90 atom of zinc per subunit of the homodimer.
soxH
coded for a periplasmic protein of 317 amino acids with a double-arginine signal peptide. The mature SoxH (32,317 Da) contained two metal binding motifs and 0.29 atom of zinc and 0.20 atom of copper per subunit of the homodimer. SoxXA, SoxYZ, SoxB, and SoxCD (C. G. Friedrich, A. Quentmeier, F. Bardischewsky, D. Rother, R. Kraft, S. Kostka, and H. Prinz, J. Bacteriol. 182:4476–4487, 2000) reconstitute a system able to perform thiosulfate-, sulfite-, sulfur-, and hydrogen sulfide-dependent cytochrome
c
reduction, and this system is the first described for oxidizing different inorganic sulfur compounds. SoxF slightly inhibited the rate of hydrogen sulfide oxidation but not the rate of sulfite or thiosulfate oxidation. From use of a homogenote mutant with an in-frame deletion in
soxF
and complementation analysis, it was evident that the
soxFGH
gene products were not required for lithotrophic growth with thiosulfate.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
119 articles.
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