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  • 1
    Electronic Resource
    Electronic Resource
    Transgenic tobacco and peas expressing a proteinase inhibitor from Nicotiana alata have increased insect resistance (1999)
    Springer
    Molecular breeding 5 (1999), S. 357-365 
    Details
    ISSN: 1572-9788
    Keywords: Helicoverpa armigera ; insect resistance ; proteinase inhibitor ; protein processing ; transgenic tobacco and pea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Proteinase inhibitors have been used to increase resistance to insect pests in transgenic plants. A cDNA clone encoding a multi-domain proteinase inhibitor precursor from Nicotiana alata (Na-PI) was transferred into tobacco and peas under the control of a promoter from a ribulose-1, 5-bisphosphate carboxylase small subunit gene. The Na-PI precursor was cleaved in the leaves of transgenic tobacco and peas, and Mr 6000 polypeptides accumulated to levels of 0.3% and 0.1%, respectively, of the total soluble protein. The Na-PI cDNA segregated as a dominant Mendelian trait and was stably transmitted for at least two generations of both species. Helicoverpa armigera larvae that ingested tobacco or pea leaves containing Na-PI exhibited higher mortality or were delayed in growth and development relative to control larvae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009633710224
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of a novel four-domain member of the proteinase inhibitor II family from the stigmas of Nicotiana alata (2000)
    Springer
    Plant molecular biology 42 (2000), S. 329-333 
    Details
    ISSN: 1573-5028
    Keywords: Nicotiana alata ; proteinase inhibitor II ; stigma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Proteinase inhibitors (PIs) of the potato type II family have been identified in a number of solanaceous species. Most family members have two PI domains which are specific for either chymotrypsin or trypsin. More recently family members have been described with three or six repeated PI domains. Here we describe a novel four-domain family member produced in the stigmas and leaves of the ornamental tobacco, Nicotiana alata, which has high sequence identity with a six-domain member from the same species. Both proteins are produced as precursors that enter the secretory pathway and are subsequently processed into a series of 6 kDa PIs. The four- and six-domain precursor proteins were isolated from immature stigmas and characterised by mass spectrometry which revealed that both proteins had been trimmed at the N-terminus, at a position corresponding to the predicted signal peptide cleavage site. Furthermore, no post-translational modifications were apparent.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006305429013
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    Paper (German National Licenses)
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