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Ahn, Namsook,Kim, Soonok,Choi, Woobong,Im, Kyung-Hwan,Lee, Yong-Hwan Korean Society for Molecular Biology 2004 Molecules and cells Vol.17 No.1
<P>Magnaporthe grisea, the causal fungus of rice blast, forms a specialized infection structure called an appressorium that is crucial for host plant penetration. A cDNA clone of M. grisea, showing strong sequence homology to FEM1 of Fusarium oxysporum and encoding an extracellular matrix protein, was isolated during an expressed sequence tag (EST) analysis of an appressorium cDNA library and named extracellular matrix protein 1 (EMP1). Sequence analysis of the corresponding genomic clone revealed that EMP1 contains an open reading frame of 685 nucleotides encoding 207 amino acids. The estimated molecular weight of the protein product was 20.5 kDa with a pI of 7.84. It contains an 18 amino acid N-terminal secretion signal sequence, as well as four potential N-glycosylation sites. At its C-terminus, the protein contains a 16 amino acid sequence with the characteristics of a glycosylphosphatidylinositol (GPI) anchor addition signal. Northern blot analysis showed that EMP1 transcripts accumulate during appressorium formation but not during vegetative growth. An EMP1 null mutant, emp1, generated by targeted gene disruption, exhibited reduced levels of appressorium formation and pathogenicity but no effect on mycelial growth rate or conidiation ability. These data suggest that EMP1 plays important roles in appressorium formation and the pathogenicity of M. grisea.</P>
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이용환,Namsook Ahn,김순옥,Woobong Choi,Kyung-Hwan Im 한국분자세포생물학회 2004 Molecules and cells Vol.17 No.1
Magnaporthe grisea, the causal fungus of rice blast, forms a specialized infection structure called an ap-pressorium that is crucial for host plant penetration. A cDNA clone of M. grisea, showing strong sequence ho-mology to FEM1 of Fusarium oxysporum and encoding an extracellular matrix protein, was isolated during an expressed sequence tag (EST) analysis of an appres-sorium cDNA library and named extracellular matrix protein 1 (EMP1). Sequence analysis of the corre-sponding genomic clone revealed that EMP1 contains an open reading frame of 685 nucleotides encoding 207 amino acids. The estimated molecular weight of the protein product was 20.5 kDa with a pI of 7.84. It con-tains an 18 amino acid N-terminal secretion signal se-quence, as well as four potential N-glycosylation sites. At its C-terminus, the protein contains a 16 amino acid sequence with the characteristics of a glycosylphos-phatidylinositol (GPI) anchor addition signal. North-ern blot analysis showed that EMP1 transcripts accu-mulate during appressorium formation but not during vegetative growth. An EMP1 null mutant, emp1, gener-ated by targeted gene disruption, exhibited reduced levels of appressorium formation and pathogenicity but no effect on mycelial growth rate or conidiation ability. These data suggest that EMP1 plays important roles in appressorium formation and the pathogenicity of M. grisea.
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Park, Joonghyuk,Ahn, Young Ock,Nam, Jeong-Won,Hong, Myoung-Ki,Song, Namsook,Kim, Taejoon,Yu, Gyung-Hee,Sung, Soon-Kee Academic Press 2018 Pesticide biochemistry and physiology Vol.152 No.-
<P><B>Abstract</B></P> <P>We conducted biochemical and physiological experiments to investigate the mode of action of tiafenacil (Terrad'or™), a new protoporphyrinogen IX oxidase (PPO)-inhibiting pyrimidinedione herbicide. Analysis of the half-maximal inhibitory concentration (IC<SUB>50</SUB>) against recombinant PPO enzymes from various plant species, including amaranth (<I>Amaranthus tuberculatus</I>), soybean (<I>Glycine</I> max), arabidopsis (<I>Arabidopsis thaliana</I>), and rapeseed (<I>Brassica napus</I>), showed that tiafenacil had an IC<SUB>50</SUB> of 22 to 28 nM, similar to the pyrimidinedione herbicides butafenacil and saflufenacil and the <I>N</I>-phenylphthalimide herbicide flumioxazin. By contrast, tiafenacil exhibited 3- to 134-fold lower IC<SUB>50</SUB> values than the diphenyl ether herbicides fomesafen, oxyfluorfen, and acifluorfen. Tiafenacil is non-selective and is herbicidal to both dicots and monocots, such as the weeds velvetleaf (<I>Abutilon theophrasti</I>), amaranth, and barnyardgrass (<I>Echinochloa crus-galli</I>) as well as the crops soybean, rapeseed, rice (<I>Oryza sativa</I>), and maize (<I>Zea mays</I>) at concentrations ranging from 1 to 50 μM. Treatment of plant tissue with tiafenacil in darkness resulted in the accumulation of protoporphyrin IX. Subsequent exposure to light increased the content of malondialdehyde and significantly decreased the Fv/Fm values of chlorophyll fluorescence. The results suggest that tiafenacil is a new PPO-inhibiting pyrimidinedione herbicide.</P> <P><B>Highlights</B></P> <P> <UL> <LI> We investigated the mode of action of tiafenacil (Terrad'or™). </LI> <LI> This new pyrimidinedione herbicide inhibits protoporphyrinogen IX oxidase. </LI> <LI> Tiafenacil had a much lower IC<SUB>50</SUB> values than diphenyl ethers. </LI> <LI> Tiafenacil is non-selective and herbicidal against both monocots and dicots. </LI> <LI> Tiafenacil causes protoporphyrin IX accumulation and oxidative damage to plants. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
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