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

Tyrosine sulfation in a Gram-negative bacterium.

Author information

1
Department of Plant Pathology and the Genome Center, University of California, One Shields Ave, Davis, California 95616, USA.

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.

PMID:
23093190
PMCID:
PMC4305400
DOI:
10.1038/ncomms2157
[Indexed for MEDLINE]
Free PMC Article

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