scholarly journals Regulation of Dissimilatory Sulfur Oxidation in the Purple Sulfur Bacterium Allochromatium Vinosum

2011 ◽  
Vol 2 ◽  
Author(s):  
Frauke Grimm ◽  
Bettina Franz ◽  
Christiane Dahl
Keyword(s):  
Sulfur Oxidation ◽  
Allochromatium Vinosum ◽  
Purple Sulfur Bacterium

scholarly journals A Comparative Quantitative Proteomic Study Identifies New Proteins Relevant for Sulfur Oxidation in the Purple Sulfur Bacterium Allochromatium vinosum

2014 ◽  
Vol 80 (7) ◽  
pp. 2279-2292 ◽  
Author(s):  
Thomas Weissgerber ◽  
Marc Sylvester ◽  
Lena Kröninger ◽  
Christiane Dahl
Keyword(s):  
Sulfur Metabolism ◽  
Sulfur Oxidation ◽  
Hypothetical Protein ◽  
Mrna Levels ◽  
Reduced Sulfur Compounds ◽  
Allochromatium Vinosum ◽  
Purple Sulfur Bacterium ◽  
Content Type ◽  
Protein Levels ◽  
New Genes

ABSTRACTIn the present study, we compared the proteome response ofAllochromatium vinosumwhen growing photoautotrophically in the presence of sulfide, thiosulfate, and elemental sulfur with the proteome response when the organism was growing photoheterotrophically on malate. Applying tandem mass tag analysis as well as two-dimensional (2D) PAGE, we detected 1,955 of the 3,302 predicted proteins by identification of at least two peptides (59.2%) and quantified 1,848 of the identified proteins. Altered relative protein amounts (≥1.5-fold) were observed for 385 proteins, corresponding to 20.8% of the quantifiedA. vinosumproteome. A significant number of the proteins exhibiting strongly enhanced relative protein levels in the presence of reduced sulfur compounds are well documented essential players during oxidative sulfur metabolism, e.g., the dissimilatory sulfite reductase DsrAB. Changes in protein levels generally matched those observed for the respective relative mRNA levels in a previous study and allowed identification of new genes/proteins participating in oxidative sulfur metabolism. One gene cluster (hyd; Alvin_2036-Alvin_2040) and one hypothetical protein (Alvin_2107) exhibiting strong responses on both the transcriptome and proteome levels were chosen for gene inactivation and phenotypic analyses of the respective mutant strains, which verified the importance of the so-called Isp hydrogenase supercomplex for efficient oxidation of sulfide and a crucial role of Alvin_2107 for the oxidation of sulfur stored in sulfur globules to sulfite. In addition, we analyzed the sulfur globule proteome and identified a new sulfur globule protein (SgpD; Alvin_2515).

scholarly journals DsrR, a Novel IscA-Like Protein Lacking Iron- and Fe-S-Binding Functions, Involved in the Regulation of Sulfur Oxidation in Allochromatium vinosum

2010 ◽  
Vol 192 (6) ◽  
pp. 1652-1661 ◽  
Author(s):  
Frauke Grimm ◽  
John R. Cort ◽  
Christiane Dahl
Keyword(s):  
Solution Structure ◽  
Sulfur Oxidation ◽  
Allochromatium Vinosum ◽  
Posttranscriptional Control ◽  
Iron Sulfur Cluster ◽  
Purple Sulfur Bacterium ◽  
Iron Sulfur ◽  
Key Enzyme ◽  
Alternative Function ◽  
Sulfur Globules

ABSTRACT In the purple sulfur bacterium Allochromatium vinosum, the reverse-acting dissimilatory sulfite reductase (DsrAB) is the key enzyme responsible for the oxidation of intracellular sulfur globules. The genes dsrAB are the first and the gene dsrR is the penultimate of the 15 genes of the dsr operon in A. vinosum. Genes homologous to dsrR occur in a number of other environmentally important sulfur-oxidizing bacteria utilizing Dsr proteins. DsrR exhibits sequence similarities to A-type scaffolds, like IscA, that partake in the maturation of protein-bound iron-sulfur clusters. We used nuclear magnetic resonance (NMR) spectroscopy to solve the solution structure of DsrR and to show that the protein is indeed structurally highly similar to A-type scaffolds. However, DsrR does not retain the Fe-S- or the iron-binding ability of these proteins, which is due to the lack of all three highly conserved cysteine residues of IscA-like scaffolds. Taken together, these findings suggest a common function for DsrR and IscA-like proteins different from direct participation in iron-sulfur cluster maturation. An A. vinosum ΔdsrR deletion strain showed a significantly reduced sulfur oxidation rate that was fully restored upon complementation with dsrR in trans. Immunoblot analyses revealed a reduced level of DsrE and DsrL in the ΔdsrR strain. These proteins are absolutely essential for sulfur oxidation. Transcriptional and translational gene fusion experiments suggested the participation of DsrR in the posttranscriptional control of the dsr operon, similar to the alternative function of cyanobacterial IscA as part of the sense and/or response cascade set into action upon iron limitation.

scholarly journals Biochemical Characterization of Individual Components of the Allochromatium vinosum DsrMKJOP Transmembrane Complex Aids Understanding of Complex Function In Vivo

2010 ◽  
Vol 192 (24) ◽  
pp. 6369-6377 ◽  
Author(s):  
Fabian Grein ◽  
Inês A. C. Pereira ◽  
Christiane Dahl
Keyword(s):  
Biochemical Characterization ◽  
Sulfur Metabolism ◽  
Complex Function ◽  
Redox Potentials ◽  
Allochromatium Vinosum ◽  
Purple Sulfur Bacterium ◽  
Membrane Anchoring ◽  
Integral Proteins ◽  
First Time

ABSTRACT The DsrMKJOP transmembrane complex has a most important function in dissimilatory sulfur metabolism and consists of cytoplasmic, periplasmic, and membrane integral proteins carrying FeS centers and b- and c-type cytochromes as cofactors. In this study, the complex was isolated from the purple sulfur bacterium Allochromatium vinosum and individual components were characterized as recombinant proteins. The two integral membrane proteins DsrM and DsrP were successfully produced in Escherichia coli C43(DE3) and C41(DE3), respectively. DsrM was identified as a diheme cytochrome b, and the two hemes were found to be in low-spin state. Their midpoint redox potentials were determined to be +60 and +110 mV. Although no hemes were predicted for DsrP, it was also clearly identified as a b-type cytochrome. To the best of our knowledge, this is the first time that heme binding has been experimentally proven for a member of the NrfD protein family. Both cytochromes were partly reduced after addition of a menaquinol analogue, suggesting interaction with quinones in vivo. DsrO and DsrK were both experimentally proven to be FeS-containing proteins. In addition, DsrK was shown to be membrane associated, and we propose a monotopic membrane anchoring for this protein. Coelution assays provide support for the proposed interaction of DsrK with the soluble cytoplasmic protein DsrC, which might be its substrate. A model for the function of DsrMKJOP in the purple sulfur bacterium A. vinosum is presented.

scholarly journals Production, crystallization and preliminary crystallographic analysis ofAllochromatium vinosumthiosulfate dehydrogenase TsdA, an unusual acidophilicc-type cytochrome

2014 ◽  
Vol 70 (10) ◽  
pp. 1424-1427 ◽  
Author(s):  
José A. Brito ◽  
André Gutierres ◽  
Kevin Denkmann ◽  
Christiane Dahl ◽  
Margarida Archer
Keyword(s):  
Crystallographic Analysis ◽  
Sulfur Cycle ◽  
Monoclinic Space Group ◽  
Asymmetric Unit ◽  
Oxidative Condensation ◽  
Unit Cell Parameters ◽  
Allochromatium Vinosum ◽  
Data Set ◽  
Purple Sulfur Bacterium ◽  
Cell Parameters

The ability to perform the very simple oxidation of two molecules of thiosulfate to tetrathionate is widespread among prokaryotes. Despite the prevalent occurrence of tetrathionate formation and its well documented significance within the sulfur cycle, little is known about the enzymes that catalyze the oxidative condensation of two thiosulfate anions. To fill this gap, the thiosulfate dehydrogenase (TsdA) enzyme from the purple sulfur bacteriumAllochromatium vinosumwas recombinantly expressed inEscherichia coli, purified and crystallized, and a crystallographic data set was collected. The crystals belonged to the monoclinic space groupC2, with unit-cell parametersa= 79.2,b= 69.9,c= 57.9 Å, β = 129.3°, contained one monomer per asymmetric unit and diffracted to a resolution of 1.98 Å.

scholarly journals Conformational Complexity in the LH2 Antenna of the Purple Sulfur Bacterium Allochromatium vinosum Revealed by Hole-Burning Spectroscopy

2017 ◽  
Vol 121 (23) ◽  
pp. 4435-4446 ◽  
Author(s):  
Adam Kell ◽  
Mahboobe Jassas ◽  
Khem Acharya ◽  
Kirsty Hacking ◽  
Richard J. Cogdell ◽  
...  
Keyword(s):  
Hole Burning ◽  
Allochromatium Vinosum ◽  
Purple Sulfur Bacterium

scholarly journals Cytoplasmic Sulfurtransferases in the Purple Sulfur Bacterium Allochromatium vinosum: Evidence for Sulfur Transfer from DsrEFH to DsrC

PLoS ONE ◽  
2012 ◽  
Vol 7 (7) ◽  
pp. e40785 ◽  
Author(s):  
Yvonne Stockdreher ◽  
Sofia S. Venceslau ◽  
Michaele Josten ◽  
Hans-Georg Sahl ◽  
Inês A. C. Pereira ◽  
...  
Keyword(s):  
Allochromatium Vinosum ◽  
Purple Sulfur Bacterium ◽  
Sulfur Transfer

scholarly journals On Light-Induced Photoconversion of B800 Bacteriochlorophylls in the LH2 Antenna of the Purple Sulfur Bacterium Allochromatium vinosum

2017 ◽  
Vol 121 (43) ◽  
pp. 9999-10006 ◽  
Author(s):  
Adam Kell ◽  
Mahboobe Jassas ◽  
Kirsty Hacking ◽  
Richard J. Cogdell ◽  
Ryszard Jankowiak
Keyword(s):  
Allochromatium Vinosum ◽  
Purple Sulfur Bacterium
Sign in / Sign up

Export Citation Format

Share Document