Abstract
Rhodococcus strain IGTS8 is the most extensively studied model bacterium for biodesulfurization of fossil fuels via the non–destructive sulfur–specific 4S pathway. This strain was initially assigned to Rhodococcus rhodochrous and later to Rhodococcus erythropolis thus making its taxonomic status debatable and reflecting the limited resolution of methods available at the time. In this study, phylogenomic analyses of the whole genome sequences of strain IGTS8 and closely related rhodococci showed that R. erythropolis and Rhodococcus qingshengii are very closely related species, that Rhodococcus strain IGTS8 is a R. qingshengii strain and that several strains identified as R. erythropolis should be re-classified as R. qingshengii. The genomes of strains assigned to these species contain potentially novel biosynthetic gene clusters showing that members of these taxa should be given greater importance in the search for new antimicrobials and other industrially important biomolecules. The plasmid-borne dsz operon encoding fossil fuel desulfurization enzymes was present in R. qingshengii IGTS8 and R. erythropolis XP suggesting that it might be transferable between members of these species.
Highlights
The implementation of green and economic technologies in the petroleum industry is of increasing interest
We downloaded the genome sequences of 29 R. erythropolis and R. qingshengii strains available from GenBank and calculated digital DNA-DNA hybridization (dDDH) values against strain IGTS8 (Table 3)
The amino acid identities (AAI) value between strain IGTS8 and R. qingshengii JCM 15477T (99.31%; SD: 5.07%) was much higher than that calculated against R. erythropolis NBRC 15567T (96.67%; SD: 7.09%)
Summary
The implementation of green and economic technologies in the petroleum industry is of increasing interest. Genome Sequence of Rhodococcus Strain IGTS8 was the first bacterium to be isolated based on its unique ability to break C-S bonds of fuel-born organosulfur compounds and utilize them as a sole sulfur source (Denome et al, 1994). This discovery raised the prospect of using biocatalysts for removal of sulfur from fossil fuels via biodesulfurization (Kilbane and Bielaga, 1990; Kilbane II and Jackowski, 1992). DszA, a FMN-dependent oxidoreductase of the nitrilotriacetate monooxygenase family, converts dibenzothiophene sulfone to 2-(2 -hydroxyphenyl) benzenesulfinate which is catalytically converted to 2-hydroxybiphenyl and sulfite by the desulfinase DszB
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