scholarly journals Identification and characterization of suppressors of plant cell death (SPD) effectors from Magnaporthe oryzae

2016 ◽  
Vol 18 (6) ◽  
pp. 850-863 ◽  
Author(s):  
William Sharpee ◽  
Yeonyee Oh ◽  
Mihwa Yi ◽  
William Franck ◽  
Alex Eyre ◽  
...  
Keyword(s):  
Cell Death ◽  
Plant Cell ◽  
Magnaporthe Oryzae ◽  
Identification And Characterization

scholarly journals Identification and characterization of GRIM-1, a cell-death-associated gene product

2010 ◽  
Vol 123 (16) ◽  
pp. 2781-2791 ◽  
Author(s):  
E. R. Hofmann ◽  
S. C. Nallar ◽  
L. Lin ◽  
J. D'Cunha ◽  
D. J. Lindner ◽  
...  
Keyword(s):  
Cell Death ◽  
Gene Product ◽  
A Cell ◽  
Identification And Characterization

scholarly journals Identification and characterization of 19 predicted Myb-family DNA binding proteins in Magnaporthe oryzae concerning growth, conidiation, and pathogenicity

2021 ◽  
Author(s):  
Ya Li ◽  
Xiuxia Zheng ◽  
Mengtian Pei ◽  
Mengting Chen ◽  
Shengnan Zhang ◽  
...  
Keyword(s):  
Stress Response ◽  
Dna Binding ◽  
Magnaporthe Oryzae ◽  
Expression Profiles ◽  
Dna Binding Proteins ◽  
The Other ◽  
Genes Encoding ◽  
Identification And Characterization ◽  
Different Levels

Genes encoding for proteins containing the DNA binding Myb domain have been suggested to be important in regulating development and stress response in eukaryotes, including fungi. Magnaporthe oryzae (teleomorph Pyricularia oryzae) is considered the most destructive pathogen of rice. We screen the M. oryzae genome for all genes encoding proteins containing Myb domains since these genes could be essential during pathogenesis. We found 19 genes Myb1-19. Only a few have previously been investigated, and only one has proven to be involved in pathogenesis. We tried to delete the other 18 genes and succeeded with all except 6, five of which could be essential. RT-qPCR showed that all 19 genes are expressed during pathogenesis, although at different levels and with different expression profiles. To our surprise, only deletions of the genes encoding proteins MoMyb2, MoMyb13, and MoMyb15 showed growth, conidiation, and infection phenotypes, indicating that they are essential on their own during infection. This lack of phenotypes for the other mutants surprised us, and we extended the analysis to look for expression co-regulation and found 5 co-regulated groups of predicted proteins with Myb-domains. We point to likely compensatory regulations of the other Myb-family genes hiding the effect of many deletions. Further studies of the Myb-family genes are thus of interest since revealing the functions of these genes with a possible effect on pathogenicity since these could be targets for future measures to control M. oryzae in rice.

scholarly journals Identification and characterization of the peroxin 1 gene MoPEX1 required for infection-related morphogenesis and pathogenicity in Magnaporthe oryzae

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Shuzhen Deng ◽  
Zhuokan Gu ◽  
Nan Yang ◽  
Ling Li ◽  
Xiaofeng Yue ◽  
...  
Keyword(s):  
Magnaporthe Oryzae ◽  
Identification And Characterization

scholarly journals The identification and characterization of a new GTP-binding protein (Gbp45) involved in cell proliferation and death related to mitochondrial function

2008 ◽  
Vol 13 (4) ◽  
Author(s):  
Yukimi Kira ◽  
Manabu Nishikawa
Keyword(s):  
Cell Proliferation ◽  
Cell Death ◽  
Mitochondrial Function ◽  
Cultured Cells ◽  
Binding Protein ◽  
Immunoblot Analysis ◽  
Gtp Binding Protein ◽  
Gtp Binding ◽  
Identification And Characterization

AbstractWe describe the identification and characterization of a GTP-binding protein with a molecular weight of 45 kD (Gbp45). Gbp45 cDNA was found to overlap with a hypothetical human protein, PTD004, the sequence of which was previously deposited in the databases. The gene for PTD004 was recently found to be one of the ATPases, hOLA1 (human Obg-like ATPase 1). The Gbp45 gene encodes a protein of 396 amino acid residues. Immunocytochemical analysis and examination with GFP-tagged protein revealed that Gbp45 is primarily located in the cytosolic compartment. Immunoblot analysis showed that the Gbp45 protein is strongly expressed in the neuronal tissues and pancreas. T43N and T56N mutations resulted in a loss of Gbp45’s ability to bind to GTP and a loss of GTPase activity. In cultured cells, the transfection of wild-type Gbp45 accelerated cell proliferation, though T43N and T56N mutations induced cell death. Down-regulating Gbp45 expression decreased the cell proliferation rate and increased the rate of cell death induced by the inhibition of mitochondrial electron transport. These findings indicate that Gbp45 plays important roles in cell proliferation and death related to mitochondrial function.

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