Abstract
Lysine acylation is a rising post‐translational modification (PTM) family that includes acetylation and similar short‐chain acylations. Reversible acylation has emerged as an important regulatory mechanism coordinating metabolism in response to changes in nutrient availability and metabolic fluxes. Since the levels of lysine acylations correlate with the levels of corresponding acyl‐CoAs and syntrophic bacteria produce complex central metabolic intermediates during fatty acid and aromatic compounds degradation, we used mass spectrometry to simultaneously reveal and evaluate all the acyl‐modifications in the syntrophs Syntrophomonas wolfei and Syntrophus aciditrophicus. Detected modifications provided insights into substrate metabolism regulations in these organisms living at the thermodynamic limits of microbial growth.Support or Funding InformationThis work is funded by the US Department of Energy (UCLA Institute of Genomics and Proteomics, DE‐FC03‐02ER63421 to J. Loo) and the National Institutes of Health (R01GM085402 to J. Loo and R. Ogorzalek Loo).
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