Tyrosine sulfation in a Gram-negative bacterium

Nat Commun. 2012;3:1153. doi: 10.1038/ncomms2157.

Abstract

Tyrosine sulfation, a well-characterized post-translation modification in eukaryotes, has not previously been reported in prokaryotes. Here, we demonstrate that the RaxST protein from the Gram-negative bacterium, Xanthomonas oryzae pv. oryzae, is a tyrosine sulfotransferase. We used a newly developed sulfotransferase assay and ultraviolet photodissociation mass spectrometry to demonstrate that RaxST catalyses sulfation of tyrosine 22 of the Xoo Ax21 (activator of XA21-mediated immunity) protein. These results demonstrate a previously undescribed post-translational modification in a prokaryotic species with implications for studies of host immune responses and bacterial cell-cell communication systems.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Assays / methods
  • Photoelectron Spectroscopy / methods
  • Protein Processing, Post-Translational
  • Substrate Specificity
  • Sulfotransferases / metabolism*
  • Tyrosine / metabolism*
  • Xanthomonas / metabolism*

Substances

  • Tyrosine
  • Sulfotransferases