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Tyrosine sulfation in a Gram-negative bacterium.

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.

SUBMITTER: Han SW

PROVIDER: S-EPMC4305400 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

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Tyrosine sulfation in a Gram-negative bacterium.

Han Sang-Wook SW Lee Sang-Won SW Bahar Ofir O Schwessinger Benjamin B Robinson Michelle R MR Shaw Jared B JB Madsen James A JA Brodbelt Jennifer S JS Ronald Pamela C PC

Nature communications 20120101

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. ...[more]

PMID: 23093190

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