Article
Got milk? The secret life of laticifers.
Department of Biological Sciences, University of Calgary, Calgary, Alberta, T2N 1N4, Canada.
Trends in Plant Science (impact factor:
11.05).
11/2008;
13(12):631-9.
DOI:10.1016/j.tplants.2008.09.005
Source: PubMed
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Citations (0)
- Cited In (2)
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Article: cDNA Cloning and Molecular Modeling of Procerain B, a Novel Cysteine Endopeptidase Isolated from Calotropis procera.
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ABSTRACT: Procerain B, a novel cysteine protease (endopeptidase) isolated from Calotropis procera belongs to Asclepiadaceae family. Purification of the enzyme, biochemical characterization and potential applications are already published by our group. Here, we report cDNA cloning, complete amino acid sequencing and molecular modeling of procerain B. The derived amino acid sequence showed high sequence homology with other papain like plant cysteine proteases of peptidase C1A superfamily. The three dimensional structure of active procerain B was modeled by homology modeling using X-ray crystal structure of actinidin (PDB ID: 3P5U), a cysteine protease from the fruits of Actinidia arguta. The structural aspect of the enzyme is also discussed.PLoS ONE 01/2013; 8(3):e59806. · 4.09 Impact Factor -
Article: Two chitinase-like proteins abundantly accumulated in latex of mulberry show insecticidal activity.
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ABSTRACT: Plant latex is the cytoplasm of highly specialized cells known as laticifers, and is thought to have a critical role in defense against herbivorous insects. Proteins abundantly accumulated in latex might therefore be involved in the defense system. We purified latex abundant protein a and b (LA-a and LA-b) from mulberry (Morus sp.) and analyzed their properties. LA-a and LA-b have molecular masses of approximately 50 and 46 kDa, respectively, and are abundant in the soluble fraction of latex. Western blotting analysis suggested that they share sequence similarity with each other. The sequences of LA-a and LA-b, as determined by Edman degradation, showed chitin-binding domains of plant chitinases at the N termini. These proteins showed small but significant chitinase and chitosanase activities. Lectin RCA120 indicated that, unlike common plant chitinases, LA-a and LA-b are glycosylated. LA-a and LA-b showed insecticidal activities when fed to larvae of the model insect Drosophila melanogaster. Our results suggest that the two LA proteins have a crucial role in defense against herbivorous insects, possibly by hydrolyzing their chitin.BMC Biochemistry 01/2010; 11:6. · 1.99 Impact Factor
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Keywords
20 plant families
alkaloids
anatomy
bioactive natural products
cytoplasmic latex exuded
developmental patterns
effective location
evolutionary
latex-bearing plants
laticifers
morphological indicator
morphology
natural rubber
physiology
plants
polyphyletic origin
specialized metabolites