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Differentially expressed proteins in the interaction of Xanthomonas axonopodis pv. citri with leaf extract of the host plant
Author(s) -
Mehta Angela,
Rosato Yoko Bomura
Publication year - 2001
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/1615-9861(200109)1:9<1111::aid-prot1111>3.0.co;2-7
Subject(s) - biology , oxygenase , spots , elongation factor , orange (colour) , protein subunit , bacteria , proteome , gel electrophoresis , heat shock protein , atp synthase , biochemistry , gene , microbiology and biotechnology , botany , genetics , rna , ribosome , horticulture
The present study reports the expression of proteins of Xanthomonas axonopodis pv. citri in response to different growth conditions. The bacterium was cultured in the basal medium MM1 and in the presence of leaf extracts from a susceptible host plant (sweet orange) as well as a resistant (ponkan) and a nonhost plant (passion fruit). The protein profiles were analyzed by two‐dimensional gel electrophoresis (2‐DE). Twelve differential spots (induced, up‐ and down‐regulated and repressed) were observed in the protein profiles of the bacterium cultivated in citrus extract (susceptible host) when compared to that of MM1. The 2‐DE profile of the bacterium cultured in the complex medium nutrient yeast glycerol was also obtained and the comparison with that of MM1 revealed 36 differential spots. Five proteins from the different treatments were successfully N ‐terminally sequenced and the putative functions were assigned by homology searches in databases. Two constitutively expressed proteins, B4 and B5, were identified as pseudouridine synthase and elongation factor P, respectively. The large subunit of ribulose 1,5‐biphosphate carboxylase/oxygenase and a sulfate binding protein were found as specifically up‐regulated in the presence of citrus extracts. Finally, the heat shock protein G was found exclusively in the complex medium and repressed in all other media.