Author
Listed:
- Sang-Wook Han
(University of California, One Shields Ave, Davis, California 95616, USA
Chung-Ang University)
- Sang-Won Lee
(University of California, One Shields Ave, Davis, California 95616, USA
Present address: Department of Plant Molecular System Biotechnology & Crop Biotech Institute, Kyung Hee University, Yongin 446-701, Korea)
- 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
Kyung Hee University)
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.
Suggested Citation
Sang-Wook Han & Sang-Won Lee & Ofir Bahar & Benjamin Schwessinger & Michelle R. Robinson & Jared B. Shaw & James A. Madsen & Jennifer S. Brodbelt & Pamela C. Ronald, 2012.
"Tyrosine sulfation in a Gram-negative bacterium,"
Nature Communications, Nature, vol. 3(1), pages 1-5, January.
Handle:
RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms2157
DOI: 10.1038/ncomms2157
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