A gene cluster for taurine sulfur assimilation in an anaerobic human gut bacterium

Meining Xing, Yifeng Wei, Gaoqun Hua, Mengya Li, Ankanahalli N. Nanjaraj Urs, Feifei Wang, Yiling Hu, Weixiang Zhai, Yangping Liu, Ee Lui Ang, Huimin Zhao, Yan Zhang

Research output: Contribution to journalArticlepeer-review


Aminoethylsulfonate (taurine) is widespread in the environment and highly abundant in the human body. Taurine and other aliphatic sulfonates serve as sulfur sources for diverse aerobic bacteria, which carry out cleavage of the inert sulfonate C–S bond through various O2-dependent mechanisms. Taurine also serves as a sulfur source for certain strict anaerobic fermenting bacteria. However, the mechanism of C–S cleavage by these bacteria has long been a mystery. Here we report the biochemical characterization of an anaerobic pathway for taurine sulfur assimilation in a strain of Clostridium butyricum from the human gut. In this pathway, taurine is first converted to hydroxyethylsulfonate (isethionate), followed by C–S cleavage by the O2-sensitive isethionate sulfo-lyase IseG, recently identified in sulfate- and sulfite-reducing bacteria. Homologs of the enzymes described in this study have a sporadic distribution in diverse strict and facultative anaerobic bacteria, from both the environment and the taurine-rich human gut, and may enable sulfonate sulfur acquisition in certain nutrient limiting conditions.

Original languageEnglish (US)
Pages (from-to)2271-2279
Number of pages9
JournalBiochemical Journal
Issue number15
StatePublished - Aug 15 2019

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'A gene cluster for taurine sulfur assimilation in an anaerobic human gut bacterium'. Together they form a unique fingerprint.

Cite this