Cloning and functional analysis of a peroxiredoxin gene,CLasPrx,from huanglongbing pathogen Candidatus Liberibacter asiaticus
To gain insights into the process of the huanglongbing pathogen Candidatus Liberibacter asi-aticus (CLas) avoiding oxidative damage,the full-length sequence of the peroxiredoxin (Prx) gene CLasPrx was cloned and the encoded protein of the CLasPrx gene was analyzed through sequence anal-ysis,multiple sequence alignment,and phylogenetic analysis. Additionally,the expression of the CLasPrx gene in various tissues was observed by real-time quantitative PCR,and its subcellular local-ization was determined by transient expression in mesophyll cells of Nicotiana benthamiana;the activi-ty of CLasPrx in eliminating H2O2 was measured using potassium iodide method. Results showed that the CLasPrx gene was 534 bp in length and could encode a protein of 177 amino acids. A Redoxin do-main was observed to be conserved in the CLasPrx protein,and multiple sequence alignment analysis indicated that the active site of the CLasPrx protein carries the conserved motif PGAFTPTC. Phyloge-netic analysis indicated that the CLasPrx was clustered with the orthologous proteins of closely related species. The expression level of CLasPrx in the autumn shoots was significantly higher than in the spring shoots. Subcellular localization analysis indicated that CLasPrx localized in the cytoplasm of me-sophyll cells of N. benthamiana. The level of H2O2 was significantly decreased due to the overexpres-sion of the CLasPrx in N. benthamiana. This study revealed that CLasPrx might play an important role in the H2O2 scavenging process in CLas.
万方数据
维普
