חיפוש מתקדם
Nature Communications
Han, S.-W., Department of Plant Pathology, Genome Center, University of California, One Shields Ave, Davis, CA 95616, United States, Department of Integrative Plant Science, Chung-Ang University, Anseong 456-756, South Korea
Lee, S.-W., Department of Plant Pathology, Genome Center, University of California, One Shields Ave, Davis, CA 95616, United States, Department of Plant Molecular System Biotechnology, Crop Biotech Institute, Kyung Hee University, Yongin 446-701, South Korea
Bahar, O., Department of Plant Pathology, Genome Center, University of California, One Shields Ave, Davis, CA 95616, United States
Schwessinger, B., Department of Plant Pathology, Genome Center, University of California, One Shields Ave, Davis, CA 95616, United States
Robinson, M.R., Department of Chemistry and Biochemistry, 1 University Station A5300, University of Texas at Austin, Austin, TX 78712-0165, United States
Shaw, J.B., Department of Chemistry and Biochemistry, 1 University Station A5300, University of Texas at Austin, Austin, TX 78712-0165, United States
Madsen, J.A., Department of Chemistry and Biochemistry, 1 University Station A5300, University of Texas at Austin, Austin, TX 78712-0165, United States
Brodbelt, J.S., Department of Chemistry and Biochemistry, 1 University Station A5300, University of Texas at Austin, Austin, TX 78712-0165, United States
Ronald, P.C., Department of Plant Pathology, Genome Center, University of California, One Shields Ave, Davis, CA 95616, United States, Department of Plant Molecular System Biotechnology, Crop Biotech Institute, Kyung Hee University, Yongin 446-701, South Korea
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. © 2012 Macmillan Publishers Limited. All rights reserved.
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תנאי שימוש
Tyrosine sulfation in a Gram-negative bacterium
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Han, S.-W., Department of Plant Pathology, Genome Center, University of California, One Shields Ave, Davis, CA 95616, United States, Department of Integrative Plant Science, Chung-Ang University, Anseong 456-756, South Korea
Lee, S.-W., Department of Plant Pathology, Genome Center, University of California, One Shields Ave, Davis, CA 95616, United States, Department of Plant Molecular System Biotechnology, Crop Biotech Institute, Kyung Hee University, Yongin 446-701, South Korea
Bahar, O., Department of Plant Pathology, Genome Center, University of California, One Shields Ave, Davis, CA 95616, United States
Schwessinger, B., Department of Plant Pathology, Genome Center, University of California, One Shields Ave, Davis, CA 95616, United States
Robinson, M.R., Department of Chemistry and Biochemistry, 1 University Station A5300, University of Texas at Austin, Austin, TX 78712-0165, United States
Shaw, J.B., Department of Chemistry and Biochemistry, 1 University Station A5300, University of Texas at Austin, Austin, TX 78712-0165, United States
Madsen, J.A., Department of Chemistry and Biochemistry, 1 University Station A5300, University of Texas at Austin, Austin, TX 78712-0165, United States
Brodbelt, J.S., Department of Chemistry and Biochemistry, 1 University Station A5300, University of Texas at Austin, Austin, TX 78712-0165, United States
Ronald, P.C., Department of Plant Pathology, Genome Center, University of California, One Shields Ave, Davis, CA 95616, United States, Department of Plant Molecular System Biotechnology, Crop Biotech Institute, Kyung Hee University, Yongin 446-701, South Korea
Tyrosine sulfation in a Gram-negative bacterium
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. © 2012 Macmillan Publishers Limited. All rights reserved.
Scientific Publication
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