Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.48 (transcriptase)
 9,479 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Summary Preharvest treatment with gibberellic acid (GA(3)) or its inhibitor paclobutrazol (PBZ) can reduce or increase, respectively, the susceptibility of persimmon fruits to Alternaria alternata. This was suggested to be the result of the ability of the fungus and produced endoglucanases to induce symptom development. To evaluate the importance of glucanases during A. alternata attack, five glucanase genes, corresponding to the C, F, and K families, were cloned from A. alternata using 'family-specific' oligonucleotide primers. The genes, present in a single copy, encode for exoglucanases AaC1 and AaC2, endoxylanase AaF1, endoglucanase AaK1, and the mixed-linked glucanase AaMLG1. Reverse transcriptase polymerase chain reaction (RT-PCR) analysis of RNA extracted from persimmon fruits, 2 and 4 days post-infection with A. alternata, showed the expression of all five glucanase genes in GA3- and PBZ-treated fruits. However, transcription levels and enzyme production of the endoglucanase (AaK1) and one exoglucanase (AaC1) were enhanced during A. alternata growth on cell walls from susceptible PBZ-treated fruits, whereas the expression of these genes and their enzyme production were significantly reduced in resistant GA(3)-treated fruits. The present results suggest the involvement of endo- and exoglucanase in symptom development caused by A. alternata in resistant and susceptible persimmon fruits.
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PMID:Characterization of Alternaria alternata glucanase genes expressed during infection of resistant and susceptible persimmon fruits. 2056 42

Understanding soil fungal distribution and activities, particularly at the level of gene expression, is important in unveiling mechanisms regulating their activities in situ. Recent identification of fungal genes involved in carbon cycling has provided the foundation for developing reverse-transcriptase PCR assays to monitor spatiotemporal gene expression patterns in soils and other complex microbial systems. The polyadenylated 3' ends of eukaryotic mRNA transcripts enables the use of oligo(dT) primers for cDNA synthesis, but this can result in the overrepresentation of the 3' end of transcripts in cDNA pools. In an effort to increase the uniformity of transcripts represented in cDNA pools, random hexamers have been used. The use of both priming methods is abundant in the literature, but we do not know how these methods perform relative to each other. We performed comparative richness and compositional analyses of the fungal glycosyl hydrolase family 7 cellobiohydrolase I gene cbhI amplified from soil cDNAs that had been generated using either oligo(dT) primers or random hexamers. Our results demonstrate that similar cbhI richness and composition were recovered using both approaches. Richness estimates and compositional profiles of cbhI sequence libraries generated from random hexamer-primed cDNA were more variable than from libraries generated from oligo(dT) primed cDNA. However, our overall results indicate that, on average, comparable richness and composition were recovered from soil cDNAs when either priming method was used.
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PMID:Comparative assessment of fungal cellobiohydrolase I richness and composition in cDNA generated using oligo(dT) primers or random hexamers. 2217 29

Upon infection, phytopathogenic fungi secrete an array of hydrolytic enzymes that can degrade components of the host epidermis, including waxes, the cuticle, and cell walls. Cellulases, which can hydrolyze crystalline cellulose in the plant cell wall, are among these hydrolytic enzymes. Here, we provide RNAi-based evidence to show that cellulases belonging to glycosyl hydrolase (GH) families 6 and 7 contribute to the penetration of the host epidermis and further invasion by the phytopathogenic fungus Magnaporthe oryzae. The GH6 and GH7 cellulases likely include all members of the cellobiohydrolase family and some endoglucanases in M. oryzae. Quantitative reverse-transcriptase polymerase chain reaction analysis indicated that more than half of the cellulases were highly induced during infection. We constructed knock-down (KD) mutants of these cellulases using the building blocks method we reported previously. The transcript levels of the target genes and cellulase activity were considerably reduced in the KD mutants. The KD mutants resulted in fewer lesions, less penetration, and infection of fewer cells compared with the parent strain. Cytological analyses showed that a high rate of papilla formation blocked invasion of the KD mutants into host cells. These results suggest that the GH6 and GH7 cellulases play roles in the virulence of M. oryzae.
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PMID:Cellulases belonging to glycoside hydrolase families 6 and 7 contribute to the virulence of Magnaporthe oryzae. 2285 7