The acyl-proteome of Syntrophus aciditrophicus reveals metabolic relationship with benzoate degradation

ABSTRACT: Syntrophus aciditrophicus is a model syntrophic bacterium that degrades fatty and aromatic acids into acetate, CO2, formate and H2 that are utilized by methanogens and other hydrogen-consuming microbes. The degradation of benzoate by S. aciditrophicus proceeds by a multi-step pathway that involves many reactive acyl-Coenzyme A species (RACS) as intermediates which can potentially result in Nε-acylation of lysine residues in proteins. Herein, we investigate post-translational modifications in the S. aciditrophicus proteome to identify and characterize a variety of acyl-lysine modifications that correspond to RACS present in the benzoate degradation pathway. Modification levels are sufficient to support post-translational modification analyses without antibody enrichment, enabling the study of a range of acylations located, presumably, on the most extensively acylated proteins. Seven types of acyl modifications were identified throughout the proteome, six of which correspond directly to RACS that are intermediates in the benzoate degradation pathway. Benzoate–degrading proteins are heavily represented among acylated proteins. The presence of functional deacylase enzymes in S. aciditrophicus indicates a potential regulatory system/mechanism by which these bacteria modulate acylation. Uniquely, Nε-acyl-lysine RACS are highly abundant in these syntrophic bacteria, raising the compelling possibility of enzyme modulation during benzoate degradation in this, and potentially, other syntrophic bacteria. Our results outline candidates to further study the impact of acylations within syntrophic systems.

INSTRUMENT(S): QSTAR

ORGANISM(S): Syntrophus Aciditrophicus Sb

SUBMITTER: Janine Fu  

LAB HEAD: Joseph A. Loo

PROVIDER: PXD025631 | Pride | 2022-03-16

REPOSITORIES: Pride