(157bj) Persulfide and Polysulfide-Induced Posttranslational Protein Modifications in Oleaginous Rhodococcus Jostii RHA1

Persulfides and polysulfides are biosynthesized endogenously and reported to be particularly nucleophilic and reducing. The formation of posttranslational modifications (PTM) on protein thiols of these compounds may play an important role in redox signaling, regulation, mitochondrial bioenergetics, etc. Oleaginous bacteria Rhodococcus sp. is one of the promising candidates for lignocellulosic biomass valorization to lipid-based biofuel. It was previously reported that another level of lipogenesis regulation through redox-mediated thiol modifications. On the other hand, the catabolism of lignin and lignin-derived aromatics will induce cellular oxidative stress response as well. In this study, we aim to globally profile persulfide or polysulfide-modifications on protein thiols using mass spectrometry in Rhodococcus jostii RHA1. The potential landscape of sulfur-containing PTMs and their regulation may shed new insights into the regulation relevant to lipogenesis.