Tyrosine sulfation in a Gram-negative bacterium

Sang-Wook Han, Sang-Won Lee, Ofir Bahar, Benjamin Schwessinger, Michelle R. Robinson, Jared B. Shaw, James A. Madsen, Jennifer S. Brodbelt and Pamela C. Ronald ()
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Sang-Wook Han: University of California, One Shields Ave, Davis, California 95616, USA
Sang-Won Lee: University of California, One Shields Ave, Davis, California 95616, USA
Ofir Bahar: University of California, One Shields Ave, Davis, California 95616, USA
Benjamin Schwessinger: University of California, One Shields Ave, Davis, California 95616, USA
Michelle R. Robinson: 1 University Station A5300, University of Texas at Austin
Jared B. Shaw: 1 University Station A5300, University of Texas at Austin
James A. Madsen: 1 University Station A5300, University of Texas at Austin
Jennifer S. Brodbelt: 1 University Station A5300, University of Texas at Austin
Pamela C. Ronald: University of California, One Shields Ave, Davis, California 95616, USA

Nature Communications, 2012, vol. 3, issue 1, 1-5

Abstract: 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.

Date: 2012
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DOI: 10.1038/ncomms2157

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