scholarly journals Crystal Structure of Chaperonin GroEL from Xanthomonas oryzae pv. oryzae

Crystals ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 399 ◽  
Author(s):  
Huyen-Thi Tran ◽  
Jongha Lee ◽  
Hyunjae Park ◽  
Jeong-Gu Kim ◽  
Seunghwan Kim ◽  
...  

Xanthomonas oryzae pv. oryzae (Xoo) is a plant pathogen that causes bacterial blight of rice, with outbreaks occurring in most rice-growing countries. Thus far, there is no effective pesticide against bacterial blight. Chaperones in bacterial pathogens are important for the stabilization and delivery of effectors into host cells to cause disease. In bacteria, GroEL/GroES complex mediates protein folding and protects proteins against misfolding and aggregation caused by environmental stress. We determined the crystal structure of GroEL from Xanthomonas oryzae pv. oryzae (XoGroEL) at 3.2 Å resolution, which showed the open form of two conserved homoheptameric rings stacked back-to-back. In the open form structure, the apical domain of XoGroEL had a higher B factor than the intermediate and equatorial domains, indicating that the apical domain had a flexible conformation before the binding of substrate unfolded protein and ATP. The XoGroEL structure will be helpful in understanding the function and catalytic mechanism of bacterial chaperonin GroELs.

2010 ◽  
Vol 23 (7) ◽  
pp. 893-902 ◽  
Author(s):  
Congfeng Song ◽  
Bing Yang

Xanthomonas oryzae pv. oryzae depends on a type III secretion system (T3SS) to translocate effectors into host cells for its ability to cause bacterial blight of rice. All type III (T3) effectors with known function in X. oryzae pv. oryzae belong to a family of transcription activator-like (TAL) effectors. However, other, non–TAL-related effector genes are present in the genome, although their role in virulence and their mode of action have yet to be elucidated. Here, we report the generation of mutants for 18 non-TAL T3 effector genes and the identification of one that contributes to the virulence of strain PXO99A. XopZPXO99 encodes a predicted 1,414-amino-acid protein of unknown function. PXO99A contains two identical copies of the gene due to a duplication of 212 kb in the genome. Strains with knockout mutations of one copy of XopZPXO99 did not exhibit any visible virulence defect. However, strains with mutations in both copies of XopZPXO99 displayed reduced virulence in terms of lesion length and bacterial multiplication compared with PXO99A. The introduction of one genomic copy of XopZPXO99 restores the mutant to full virulence. Transient expression of XopZPXO99 in Nicotiana benthamiana leaves suppresses host basal defense, which is otherwise induced by a T3SS mutant of PXO99A, suggesting a role for XopZPXO99 in interfering with host innate immunity during X. oryzae pv. oryzae infection. XopZPXO99-related genes are found in all Xanthomonas spp. whose genomic sequences have been determined, suggesting a conserved role for this type of effector gene in pathogenesis of Xanthomonas spp. Our results indicate that XopZPXO99 encodes a novel T3 effector and contributes virulence to X. oryzae pv. oryzae strains for bacterial blight of rice.


2019 ◽  
Vol 109 (11) ◽  
pp. 1869-1877
Author(s):  
Yuqiang Zhang ◽  
Guichun Wu ◽  
Ian Palmer ◽  
Bo Wang ◽  
Guoliang Qian ◽  
...  

The plant bacterial pathogen Xanthomonas oryzae pv. oryzae causes bacterial blight of rice, which is one of the most destructive rice diseases prevalent in Asia and parts of Africa. Despite many years of research, how X. oryzae pv. oryzae causes bacterial blight of rice is still not completely understood. Here, we show that the loss of the rocF gene caused a significant decrease in the virulence of X. oryzae pv. oryzae in the susceptible rice cultivar IR24. Bioinformatics analysis demonstrated that rocF encodes arginase. Quantitative real-time PCR and Western blot assays revealed that rocF expression was significantly induced by rice and arginine. The rocF deletion mutant strain showed elevated sensitivity to hydrogen peroxide, reduced extracellular polysaccharide (EPS) production, and reduced biofilm formation, all of which are important determinants for the full virulence of X. oryzae pv. oryzae, compared with the wild-type strain. Taken together, the results of this study revealed a mechanism by which a bacterial arginase is required for the full virulence of X. oryzae pv. oryzae on rice because of its contribution to tolerance to reactive oxygen species, EPS production, and biofilm formation.


2020 ◽  
Vol 149 ◽  
pp. 104559
Author(s):  
Kumari Vishakha ◽  
Shatabdi Das ◽  
Satarupa Banerjee ◽  
Sandhimita Mondal ◽  
Arnab Ganguli

Plant Disease ◽  
2020 ◽  
Vol 104 (11) ◽  
pp. 2764-2767
Author(s):  
Zhengyin Xu ◽  
Sai Wang ◽  
Liang Liu ◽  
Yangyang Yang ◽  
Bo Zhu ◽  
...  

Xanthomonas oryzae pv. oryzae is the causative agent of bacterial blight of rice and causes severe harvest loss and challenges to a stable food supply globally. In this study, a hypervirulent strain, LN4, compatible in rice varieties carrying Xa3, Xa4, xa13, and xa25 resistance genes, was used to generate DNA for nanopore sequencing. After assembly, the genome comprises a single chromosome of 5,012,583 bp, consisting of a total of 6,700 predicted coding sequences. Seventeen transcription activator-like effectors (TALEs) were encoded in the genome, of which two (Tal7 and Tal6c) were major TALEs. The approach and genome data provide information for the discovery of new virulence effectors and understanding of the virulence mechanism of TALEs in rice.


2017 ◽  
Vol 68 (5) ◽  
pp. 434
Author(s):  
Thien-Hoang Ho ◽  
Myoung-Ki Hong ◽  
Seunghwan Kim ◽  
Jeong-Gu Kim ◽  
Jongha Lee ◽  
...  

Xanthomonas oryzae pv. oryzae (Xoo) is the causal agent of bacterial blight of rice, one of the most devastating rice diseases. We analysed the time-resolved transcriptional expression of aminoacyl-tRNA synthetase (aaRS) genes in Xoo cells treated with rice-leaf extract. Most aaRS genes showed decreased expression in the initial 30 min and recovered or increased expression in the later 30 min. The protein-synthetic machinery of bacterial cells is an important target for developing antibiotic agents; aaRSs play an essential role in peptide synthesis by attaching amino acids onto the corresponding tRNA. In bacteria, glutaminyl-tRNA (Gln-tRNAGln) is synthesised in two steps by glutamyl-tRNA synthetase (GluRS) and tRNA-dependent aminotransferase, the indirect biosynthetic mechanism of which is not present in eukaryotes. We determined the crystal structure of GluRS from Xoo (XoGluRS) at resolution of 3.0 Å, this being the first GluRS structure from a plant pathogen such as Xoo. The XoGluRS structure consists of five domains, which are conserved in other bacterial GluRS structures. In the bacterial GluRS structures, the Rossmann-fold catalytic domain and the stem-contact domain are most conserved in both sequence and structure. The anticodon-binding domain 1 is less conserved in sequence but overall structure is conserved. The connective-polypeptide domain and the anticodon-binding domain 2 show various conformations in structure. The XoGluRS structure could provide useful information to develop a new pesticide against Xoo and bacterial blight.


2012 ◽  
Vol 8 (11) ◽  
pp. 504-507 ◽  
Author(s):  
Vidavaluru Sravani Reddy ◽  
Yellapu Nanda Kumar ◽  
Aminedi Raghavendra ◽  
Gopal Sowjenya ◽  
Suman Kumar ◽  
...  

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