Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.15 (pectinase)
 2,440 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Natural rubber, cis-1,4-polyisoprene, is obtained from a colloidal fluid called latex, which represents the cytoplasmic content of the laticifers of the rubber tree (Hevea brasiliensis). We have developed a method of extracting translatable mRNA from freshly tapped latex. Analysis of in vitro translation products of latex mRNA showed that the encoded polypeptides are very different from those of leaf mRNA and these differences are visible in the protein profiles of latex and leaf as well. Northern blot analysis demonstrated that laticifer RNA is 20- to 100-fold enriched in transcripts encoding enzymes involved in rubber biosynthesis. Plant defense genes encoding chitinases, pathogenesis-related protein, phenylalanine ammonia-lyase, chalcone synthase, chalcone isomerase, cinnamyl alcohol dehydrogenase, and 5-enolpyruvylshikimate-3-phosphate synthase show a 10- to 50-fold higher expression in laticifers than in leaves, indicating the probable response of rubber trees to tapping and ethylene treatment. Photosynthetic genes encoding ribulose-bisphosphate carboxylase small subunit and chlorophyll a/b-binding protein are not expressed at a detectable level in laticifers. In contrast, genes encoding two hydrolytic enzymes, cellulase and polygalacturonase, are more highly expressed in laticifers than in leaves. Transcripts for the cytoplasmic form of glutamine synthase are preferentially expressed in laticifers, whereas those for the chloroplastic form of the same enzyme are present mainly in leaves. Control experiments demonstrated that beta-ATPase, actin, and ubiquitin are equally expressed in laticifers and leaves. Therefore, the differences in specific transcript abundance between laticifers and leaves are due to differential expression of the genes for these transcripts in the laticifers.
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PMID:Laticifer-specific gene expression in Hevea brasiliensis (rubber tree). 1160 69

Plant polygalacturonase-inhibiting protein (PGIP) is a structural protein that can specifically recognize and bind to fungal polygalacturonase (PG). PGIP plays an important role in plant antifungal activity. In this study, a maize PGIP gene, namely ZmPGIP3, was cloned and characterized. Agarose diffusion assay suggested that ZmPGIP3 could inhibit the activity of PG. ZmPGIP3 expression was significantly induced by wounding, Rhizoctonia solani infection, jasmonate, and salicylic acid. ZmPGIP3 might be related to disease resistance. The gene encoding ZmPGIP3 was posed under the control of the ubiquitin promoter and constitutively expressed in transgenic rice. In an R. solani infection assay, ZmPGIP3 transgenic rice was more resistant to sheath blight than the wild-type rice regardless of the inoculated plant part (leaves or sheaths). Digital gene expression analysis indicated that the expression of some rice PGIP genes significantly increased in ZmPGIP3 transgenic rice, suggesting that ZmPGIP3 might activate the expression of some rice PGIP genes to resist sheath blight. Our investigation of the agronomic traits of ZmPGIP3 transgenic rice showed that ZmPGIP3 overexpression in rice did not show any detrimental phenotypic or agronomic effect. ZmPGIP3 is a promising candidate gene in the transgenic breeding for sheath blight resistance and crop improvement.
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PMID:ZmPGIP3 Gene Encodes a Polygalacturonase-Inhibiting Protein that Enhances Resistance to Sheath Blight in Rice. 3147 3