AI Article Synopsis

  • The purple sulfur bacterium BBS has a thermostable enzyme called HydSL hydrogenase, crucial for hydrogen activation and sulfur reduction.
  • It has a unique genomic structure that needs to be fully sequenced to confirm its relation to sulfur metabolism.
  • The complete genome has been assembled, revealing insights into its metabolic functions and identifying key genes for sulfur metabolism and pigment biosynthesis compared to another related bacterium, DSM 180T.

Article Abstract

The purple sulfur bacterium BBS is interesting from both fundamental and practical points of view. It possesses a thermostable HydSL hydrogenase, which is involved in the reaction of reversible hydrogen activation and a unique reaction of sulfur reduction to hydrogen sulfide. It is a very promising enzyme for enzymatic hydrogenase electrodes. There are speculations that HydSL hydrogenase of purple bacteria is closely related to sulfur metabolism, but confirmation is required. For that, the full genome sequence is necessary. Here, we sequenced and assembled the complete genome of this bacterium. The analysis of the obtained whole genome, through an integrative approach that comprised estimating the Average Nucleotide Identity (ANI) and digital DNA-DNA hybridization (DDH) parameters, allowed for validation of the systematic position of as BBS. For the first time, we have assembled the whole genome of this typical strain of a new bacterial species and carried out its functional description against another purple sulfur bacterium: DSM 180T. We refined the automatic annotation of the whole genome of the bacteria BBS and localized the genomic positions of several studied genes, including those involved in sulfur metabolism and genes encoding the enzymes required for the TCA and glyoxylate cycles and other central metabolic pathways. Eleven additional genes coding proteins involved in pigment biosynthesis was found.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10892978PMC
http://dx.doi.org/10.3390/microorganisms12020391DOI Listing

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