Sulfur oxidation in Paracoccus pantotrophus: interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein

2003 ◽  
Vol 312 (4) ◽  
pp. 1011-1018 ◽  
Author(s):  
Armin Quentmeier ◽  
Petra Hellwig ◽  
Frank Bardischewsky ◽  
Gerlinde Grelle ◽  
Regine Kraft ◽  
...  
Keyword(s):  
Binding Protein ◽  
Sulfur Oxidation ◽  
Paracoccus Pantotrophus

scholarly journals Identification of ccdA inParacoccus pantotrophus GB17: Disruption ofccdA Causes Complete Deficiency inc-Type Cytochromes

2001 ◽  
Vol 183 (1) ◽  
pp. 257-263 ◽  
Author(s):  
Frank Bardischewsky ◽  
Cornelius G. Friedrich
Keyword(s):  
Sulfur Oxidation ◽  
Open Reading Frames ◽  
Redox Mediators ◽  
Transmembrane Helices ◽  
Wild Type ◽  
Structural Identity ◽  
Paracoccus Pantotrophus ◽  
Type Gene ◽  
Extension Analysis ◽  
Reading Frames

ABSTRACT A transposon Tn5-mob insertional mutant ofParacoccus pantotrophus GB17, strain TP43, was unable to oxidize thiosulfate aerobically or to reduce nitrite anaerobically, and the cellular yields were generally decreased by 11 to 20%. Strain TP43 was unable to form functional c-type cytochromes, as determined by difference spectroscopy and heme staining. However, formation of apocytochromes and their transport to the periplasm were not affected, as seen with SoxD, a c-type cytochrome associated with the periplasmic sulfite dehydrogenase homologue. The Tn5-mob-containing DNA region of strain TP43 was cloned into pSUP205 to produce pE18TP43. With the aid of pE18TP43 the corresponding wild-type gene region of 15 kb was isolated from a heterogenote recombinant to produce pEF15. Sequence analysis of 2.8 kb of the relevant region uncovered three open reading frames, designated ORFA, ccdA, and ORFB, with the latter being oriented divergently. ORFA and ccdA were constitutively cotranscribed as determined by primer extension analysis. In strain TP43 Tn5-mob was inserted into ccdA. The deduced ORFA product showed no similarity to any protein in databases. However, the ccdA gene product exhibited similarities to proteins assigned to different functions in bacteria, such as cytochrome c biogenesis. For these proteins at least six transmembrane helices are predicted with the potential to form a channel with two conserved cysteines. This structural identity suggests that these proteins transfer reducing equivalents from the cytoplasm to the periplasm and that the cysteines bring about this transfer to enable the various specific functions via specific redox mediators such as thioredoxins. CcdA of P. pantotrophus is 42% identical to a protein predicted by ORF2, and its location within thesox gene cluster coding for lithotrophic sulfur oxidation suggested a different function.

Redox Control of Chemotrophic Sulfur Oxidation of Paracoccus pantotrophus

2008 ◽  
pp. 139-150 ◽  
Author(s):  
Cornelius G. Friedrich ◽  
Armin Quentmeier ◽  
Frank Bardischewsky ◽  
Dagmar Rother ◽  
Grazyna Orawski ◽  
...  
Keyword(s):  
Sulfur Oxidation ◽  
Redox Control ◽  
Paracoccus Pantotrophus

The flavoprotein SoxF mediates the redox-balance of chemotrophic sulfur oxidation in Paracoccus pantotrophus

2006 ◽  
Vol 2006 (Spring) ◽  
Author(s):  
Frank Bardischewsky ◽  
Cornelius Friedrich ◽  
Armin Quentmeier ◽  
Dagmar Rother ◽  
Petra Hellwig
Keyword(s):  
Sulfur Oxidation ◽  
Redox Balance ◽  
Paracoccus Pantotrophus

scholarly journals The periplasmic thioredoxin SoxS plays a key role in activation in vivo of chemotrophic sulfur oxidation of Paracoccus pantotrophus

Microbiology ◽  
2007 ◽  
Vol 153 (4) ◽  
pp. 1081-1086 ◽  
Author(s):  
G. Orawski ◽  
F. Bardischewsky ◽  
A. Quentmeier ◽  
D. Rother ◽  
C. G. Friedrich
Keyword(s):  
Sulfur Oxidation ◽  
Paracoccus Pantotrophus

SoxRS-mediated regulation of chemotrophic sulfur oxidation in Paracoccus pantotrophus

Microbiology ◽  
2005 ◽  
Vol 151 (5) ◽  
pp. 1707-1716 ◽  
Author(s):  
Dagmar Rother ◽  
Grazyna Orawski ◽  
Frank Bardischewsky ◽  
Cornelius G. Friedrich
Keyword(s):  
Sequence Analysis ◽  
Sulfur Oxidation ◽  
Growth Conditions ◽  
Kanamycin Resistance ◽  
Cysteine Residue ◽  
Mobility Shift ◽  
C Terminus ◽  
Intergenic Regions ◽  
Paracoccus Pantotrophus ◽  
Gel Mobility Shift

Paracoccus pantotrophus GB17 requires thiosulfate for induction of the sulfur-oxidizing (Sox) enzyme system. The soxRS genes are divergently oriented to the soxVWXYZA–H genes. soxR predicts a transcriptional regulator of the ArsR family and soxS a periplasmic thioredoxin. The homogenote mutant GBΩS carrying a disruption of soxS by the Ω-kanamycin-resistance-encoding interposon expressed a low thiosulfate-oxidizing activity under heterotrophic and mixotrophic growth conditions. This activity was repressed by complementation with soxR, suggesting that SoxR acts as a repressor and SoxS is essential for full expression. Sequence analysis uncovered operator characteristics in the intergenic regions soxS–soxV and soxW–soxX. In each region a transcription start site was identified by primer extension analysis. Both regions were cloned into the vector pRI1 and transferred to P. pantotrophus. Strains harbouring pRI1 with soxS–soxV or soxW–soxX expressed the sox genes under heterotrophic conditions at a low rate, indicating repressor titration. Sequence analysis of SoxR suggested a helix–turn–helix (HTH) motif at position 87–108 and uncovered an invariant Cys-80 and a cysteine residue at the C-terminus. SoxR was overproduced in Escherichia coli with an N-terminal His6-tag and purified to near homogeneity. Electrophoretic gel mobility shift assays with SoxR retarded the soxS–soxV region as a single band while the soxW–soxX region revealed at least two protein–DNA complexes. These data demonstrated binding of SoxR to the relevant DNA. This is believed to be the first report of regulation of chemotrophic sulfur oxidation at the molecular level.

scholarly journals Purification and Some Properties of a Hydrogen Sulfide-binding Protein That Is Involved in Sulfur Oxidation of Thiobacillus ferrooxidans.

1991 ◽  
Vol 55 (8) ◽  
pp. 2091-2097 ◽  
Author(s):  
Tsuyoshi Sucio ◽  
Hiroyuki SUZUKI ◽  
Aya OTO ◽  
Kenji INAGAKI ◽  
Hidehiko TANAKA ◽  
...  
Keyword(s):  
Hydrogen Sulfide ◽  
Thiobacillus Ferrooxidans ◽  
Binding Protein ◽  
Sulfur Oxidation
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