Bacterial Sulfur Globules: Occurrence, Structure and Metabolism

Dahl, Christiane; Prange, Alexander

doi:10.1007/3-540-33774-1_2

Cited by 81 publications

(55 citation statements)

References 107 publications

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“…These kind of sulfur structures are usually present either in the periplasmic compartment or in the extracellular environment (44). In any case, the chemical nature of sulfur in the globules is still a debated question, and it seems that three different forms could be found, depending on the approach used: cyclo-octasulfur (S 8 ), polythionates ([(S n SO 3 ) 2 ] 2Ϫ ), and sulfur chains (45).…”

Section: Discussionmentioning

confidence: 99%

Rhodanese Functions as Sulfur Supplier for Key Enzymes in Sulfur Energy Metabolism

Aussignargues¹,

Giuliani²,

Infossi

et al. 2012

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Rhodanese Functions as Sulfur Supplier for Key Enzymes in Sulfur Energy Metabolism

Aussignargues¹,

Giuliani²,

Infossi

et al. 2012

Journal of Biological Chemistry

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“…vinosum to the final product sulfate, sulfur globules are accumulated as an intermediate inside the cells (Brune, 1995;Dahl & Prange, 2006). The chemical nature of these globules has been determined by Prange et al (2002a) as sulfur chains (most probably terminated by organic residues at one or both ends) by X-ray absorption near-edge structure (XANES) spectroscopy.…”

Section: Introductionmentioning

confidence: 99%

“…Modrow et al, 2001;Prange et al, 2002aPrange et al, , 2005. Furthermore, XANES can distinguish between sulfur rings and chain structures of zero valent sulfur (Prange et al, 2006). While Prange et al (2002a) investigated the speciation of sulfur globules of Alc.…”

Section: Introductionmentioning

confidence: 99%

Utilization of solid ‘elemental’ sulfur by the phototrophic purple sulfur bacterium Allochromatium vinosum: a sulfur K-edge X-ray absorption spectroscopy study

et al. 2007

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“…Among them are phototrophic purple and green sulfur bacteria, chemotrophic sulfur-oxidizing bacteria, like Thiobacillus denitrificans, and several symbiotic sulfur oxidizers, like "Candidatus Ruthia magnifica" strain Cm, the endosymbiont of the deep-sea hydrothermal-vent clam Calyptogena magnifica. In many sulfur-oxidizing prokaryotes and in all of the organisms mentioned above, sulfur globules are formed as intermediates during the oxidation of sulfide or thiosulfate (16,51). The only gene region proven to be essential for the oxidation of sulfur stored in sulfur globules has been identified in the purple sulfur bacterium Allochromatium vinosum (51).…”

mentioning

confidence: 99%

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

2010

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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 proteinbound 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 ⌬dsrR 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 ⌬dsrR 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.

show abstract

Bacterial Sulfur Globules: Occurrence, Structure and Metabolism

Cited by 81 publications

References 107 publications

Rhodanese Functions as Sulfur Supplier for Key Enzymes in Sulfur Energy Metabolism

Rhodanese Functions as Sulfur Supplier for Key Enzymes in Sulfur Energy Metabolism

Utilization of solid ‘elemental’ sulfur by the phototrophic purple sulfur bacterium Allochromatium vinosum: a sulfur K-edge X-ray absorption spectroscopy study

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

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