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  • 1
    ISSN: 1432-2242
    Keywords: Randomly amplified polymorphic DNA (RAPD) ; Deletion mapping ; Sequence Tagged Site (STS) ; Monosomic fragment additions ; Beet cyst nematode resistance ; Heterodera schachtii Schm ; Beta patellaris
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A beet cyst nematode (BCN)-resistant telosomic addition of B. patellaris chromosome 1 in B. vulgaris was used to isolate 6 RAPD markers linked to the BCN resistance locus Hs1 pat-1. Southern analysis showed that the analyzed RAPD products contain either low-, middle or high-repetitive DNA. The relative positions of the random amplified polymorphic DNA (RAPD) markers and of the restriction fragment length polymorphism (RFLP) loci corresponding to the low-repetitive RAPD products were determined by deletion mapping using a panel of seven nematode-resistant B. patellaris chromosome-1 fragment additions. One RAPD marker, OPB11800, was found to be present in two copies on the long arm telosome of B. patellaris chromosome 1. These copies are closely linked to the BCN resistance gene and flank the gene on both sides. On the basis of the nucleotide sequence of OPB11800, sequence-tagged site (STS) primers were developed that amplify specific fragments derived from the two OPB11800 loci. These STS markers can be used in the map-based cloning of the BCN gene, as they define start and finishing points of a chromosomal walk towards the Hs1 pat-1 locus. Two copies of the middle-repetitive OPX21100 marker were mapped in the same interval of the deletion mapping panel as the resistance gene locus and thereby belong to the nearest markers as yet found for the BCN gene in B. patellaris.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 26 (1994), S. 25-37 
    ISSN: 1573-5028
    Keywords: Antimicrobial ; ion channel ; phosphoinositides ; plant defence ; thionins ; toxins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Thionins are low-molecular-weight proteins (M r ca. 5000) occurring in seeds, stems, roots and leaves of a number of plant species. The different members of this family of plant proteins show both sequence and structural homology, and are toxic to bacteria, fungi, yeasts and various naked cells in vitro. Toxicity requires an electrostatic interaction of the positively charged thionin with the negatively charged phospholipids making up the membrane, followed by either pore formation or a specific interaction with a certain lipid domain. This domain might be composed of phosphoinositides, which mediate transduction of environmental signals in eukaryotes. Their in vitro toxicity to plant pathogenic bacteria and fungi could reflect a direct role in plant defence, although, in view of the many divergent activities displayed by thionins both in vitro and in vivo, a biological role other than inhibition of microbial growth is equally plausible.
    Type of Medium: Electronic Resource
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