Staphylococcus aureus and bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways

Stephanie Brown, Timothy Meredith, Jonathan Swoboda, Suzanne Walker

Research output: Contribution to journalArticle

29 Scopus citations

Abstract

Wall teichoic acids (WTAs) are anionic polymers that play key roles in bacterial cell shape, cell division, envelope integrity, biofilm formation, and pathogenesis. B. subtilis W23 and S. aureus both make polyribitol-phosphate (RboP) WTAs and contain similar sets of biosynthetic genes. We use in vitro reconstitution combined with genetics to show that the pathways for WTA biosynthesis in B. subtilis W23 and S. aureus are different. S. aureus requires a glycerol-phosphate primase called TarF in order to make RboP-WTAs; B. subtilis W23 contains a TarF homolog, but this enzyme makes glycerol-phosphate polymers and is not involved in RboP-WTA synthesis. Instead, B. subtilis TarK functions in place of TarF to prime the WTA intermediate for chain extension by TarL. This work highlights the enzymatic diversity of the poorly characterized family of phosphotransferases involved in WTA biosynthesis in Gram-positive organisms.

Original languageEnglish (US)
Pages (from-to)1101-1110
Number of pages10
JournalChemistry and Biology
Volume17
Issue number10
DOIs
StatePublished - Oct 29 2010

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry

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