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Insights into the sulfur metabolism of Chlorobaculum tepidum by label-free quantitative proteomics

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Meier-Credo,  Jakob       
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;

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Langer,  Julian D.       
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;
Proteomics, Max Planck Institute for Brain Research, Frankfurt am Main, Germany;

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Citation

Lyratzakis, A., Meier-Credo, J., Langer, J. D., & Tsiotis, G. (2023). Insights into the sulfur metabolism of Chlorobaculum tepidum by label-free quantitative proteomics. Proteomics, 23(10): 2200138. doi:10.1002/pmic.202200138.


Cite as: https://hdl.handle.net/21.11116/0000-000C-999B-9
Abstract
Chlorobaculum tepidum is an anaerobic green sulfur bacterium which oxidizes sulfide, elemental sulfur, and thiosulfate for photosynthetic growth. It can also oxidize sulfide to produce extracellular S0 globules, which can be further oxidized to sulfate and used as an electron donor. Here we performed label-free quantitative proteomics on total cell lysates prepared from different metabolic states, including a sulfur production state (10 hours post incubation, PI), the beginning of sulfur consumption (20 hours PI) and the end of sulfur consumption (40 hours PI), respectively. We observed an increased abundance of the sulfide:quinone oxidoreductase Sqr proteins in 10 h PI indicating a sulfur production state. The periplasmic thiosulfate-oxidizing Sox enzymes and the dissimilatory sulfite reductase Dsr subunits showed an increased abundance in 20 h PI, corresponding to the sulfur-consuming state. In addition, we found that the abundance of the heterodisulfide-reductase and the sulfhydrogenase operons was influenced by electron donor availability and may be associated with sulfur metabolism. Further, we isolated and analyzed the extracellular sulfur globules in the different metabolic states to study their morphology and the sulfur cluster composition, yielding 58 previously uncharacterized proteins in purified globules. Our results show that Cba tepidum regulates the cellular levels of enzymes involved in sulfur metabolism in response to the availability of reduced sulfur compounds.