Deciphering the Role of Tyrosine Sulfation in Xanthomonas oryzae pv. oryzae Using Shotgun Proteomic Analysis.
A bacterial tyrosine sulfotransferase, RaxST, is required for activation of rice XA21-mediated immunity, and it catalyzes sulfation of tyrosine residues of Omp1X and RaxX in Xanthomonas oryzae pv. oryzae, a causal agent of bacterial blight in rice. Although RaxST is biochemically well-characterized, biological functions of tyrosine sulfation have not been fully elucidated. We compared protein expression patterns between the wildtype and a raxST knockout mutant using shotgun proteomic analysis. Forty nine proteins displayed a more than 1.5-fold difference in their expression between the wildtype and the mutant strains. Clusters of orthologous groups analysis revealed that proteins involved in cell motility were most abundant, and phenotypic observation also showed that the twitching motility of the mutant was dramatically changed. These results indicate that tyrosine sulfation by RaxST is essential for Xoo movement, and they provide new insights into the biological roles of RaxST in cellular processes.
Department of Integrative Plant Science, Chung-Ang University, Anseong 17546, Korea.
Hye-Jee
HJ
Park
Department of Plant Biotechnology and Plant Engineering Research Institute, Sejong University, Seoul 05006, Korea.
Chang-Jin
CJ
Park
Department of Integrative Plant Science, Chung-Ang University, Anseong 17546, Korea.
Nahee
N
Bae
Department of Integrative Plant Science, Chung-Ang University, Anseong 17546, Korea.
Sang-Wook
SW
Han
Xanthomonas oryzae pv. oryzae; proteomics; tyrosine sulfation