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  • 1
    Electronic Resource
    Electronic Resource
    External association of hordothionin with protein bodies in mature barley (1980)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 28 (1980), S. 399-402 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60228a018
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  • 2
    Electronic Resource
    Electronic Resource
    The Erwinia chrysanthemi phoP-phoQ operon plays an important role in growth at low pH, virulence and bacterial survival in plant tissue (2003)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 49 (2003), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We have studied the role of acidic pH as a barrier for the colonization of the plant apoplast by Erwinia chrysanthemi. A minitransposon containing a promoterless reporter gene, gus, was used for random mutagenesis of the bacterial genome. An acid-sensitive mutant, named BT119, was isolated and had the following differential features with respect to the wild-type strain: (i) inability to grow at pH ≤ 5.5; (ii) decreased survival at acid pH and in plant tissues; (iii) increased susceptibility to antimicrobial peptides; (iv) decreased virulence in chicory leaves and pear fruits; (v) reduced polygalacturonase production; and (vi) reduced ability to alkalinize chicory tissues after infection. The sequence of the interrupted gene was highly similar to the phoQ gene, which is involved in environmental sensing in several bacteria, such as Yersinia pseudotuberculosis, Erwinia carotovora, Salmonella typhimurium and Escherichia coli and thus, this designation was used for the E. chrysanthemi system. This gene was induced at low Mg2+ concentrations and in planta. These results suggest that E. chrysanthemi PhoP-PhoQ system plays an important role in bacterial survival in plant tissues during the initial infection stages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2003.03583.x
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  • 3
    Electronic Resource
    Electronic Resource
    Genetics of Synthesis of β-Sitosterol Esters in Wheat and Related Species (1968)
    [s.l.] : Nature Publishing Group
    Nature 220 (1968), S. 1144-1145 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1. /5-Sitosterol ester patterns of T. carthlicum, synthetic T. (T. carthlicum x Ae. squarrosa), Ae. squarrosa, T. aestivum and T. durum. Separation method as described by Gilles and Young1. In an extensive survey of T. durum and T. aestivum varieties2, no P-L pattern was found in the first ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2201144a0
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  • 4
    Electronic Resource
    Electronic Resource
    Linearization of the BCK-logic (2000)
    Springer
    Studia logica 65 (2000), S. 31-51 
    Details
    ISSN: 1572-8730
    Keywords: BCK algebras ; chains ; linearization ; algebraizable logic
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics , Philosophy
    Notes: Abstract In the paper we obtain a new characterization of the BCK-algebras which are subdirect product of BCK-chains. We give an axiomatic algebraizable extension of the BCK-calculus, by means of a recursively enumerable set of axioms, such that its equivalent algebraic semantics is definitionally equivalent to the quasivariety of BCK-algebras generated by the BCK-chains. We propose the concept of "linearization of a system" and we give some examples.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005290924926
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  • 5
    Electronic Resource
    Electronic Resource
    Site-directed mutagenesis and expression inEscherichia coli of WMAI-1, a wheat monomeric inhibitor of insect α-amylase (1991)
    Springer
    Plant molecular biology 17 (1991), S. 1005-1011 
    Details
    ISSN: 1573-5028
    Keywords: α-amylase inhibitor ; expression inE. coli ; glycosylation versus activity ; insect α-amylase ; mutagenesis ; wheat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The wheat monomeric inhibitor WMAI-1 (syn. 0.28) produced inEscherichia coli using the pT7-7 expression ventor has the correct N-terminal sequence and the same electrophoretic mobility and specific activity towards the α-amylase from the insectTenebrio molitor as the native WMAI-1 isolated from wheat. This confirms that the native inhibitor is not glycosylated and contradicts claims that a putative glycosyl moiety was essential for inhibition. Thirteen mutants have been obtained at six different sites. Substitution of the highly conserved N-terminal S by the sequence ARIRAR increased the pre-incubation time required for maximum activity. A similar result was obtained by insertion of GPRLPW after position 4, while insertion of EPRAPW at the same position rendered the inhibitor inactive. The substitution D/EGPRL and insertions DGP or D, at position 58, produced complete inactivation. All other mutations had only minor effects on activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00037140
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  • 6
    Electronic Resource
    Electronic Resource
    Cloning of cDNA and chromosomal location of genes encoding the three types of subunits of the wheat tetrameric inhibitor of insect α-amylase (1990)
    Springer
    Plant molecular biology 14 (1990), S. 845-853 
    Details
    ISSN: 1573-5028
    Keywords: α-amylase tetrameric inhibitor ; cDNA cloning ; genetic mapping ; wheat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have characterized three cDNA clones corresponding to proteins CM1, CM3 and CM16, which represent the three types of subunits of the wheat tetrameric inhibitor of insect α-amylases. The deduced amino acid sequences of the mature polypeptides are homologous to those of the dimeric and monomeric α-amylase inhibitors and of the trypsin inhibitors. The mature polypeptides are preceded by typical signal peptides. Southern blot analysis of appropriate aneuploids, using the cloned cDNAs as probes, has revealed the location of genes for subunits of the CM3 and of the CM16 type within a few kb of each other in chromosomes 4A, 4B and 4D, and those for the CM1 type of subunit in chromosomes 7A, 7B and 7D. Known subunits of the tetrameric inhibitor corresponding to genes from the B and D genomes have been previously characterized. No proteins of this class have been found to be encoded by the A genome in hexaploid wheat (genomes AA, BB, DD) or in diploid wheats (AA) and no anti α-amylase activity has been detected in the latter, so that the A-genome genes must be either silent (pseudogenes) or expressed at a much lower level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00016517
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  • 7
    Electronic Resource
    Electronic Resource
    Differential expression of pathogen-responsive genes encoding two types of glycine-rich proteins in barley (1997)
    Springer
    Plant molecular biology 33 (1997), S. 803-810 
    Details
    ISSN: 1573-5028
    Keywords: barley ; cold ; ethylene ; glycine-rich proteins ; methyl-jasmonate ; pathogen infection
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Gene-specific probes (3' ends of cDNAs) were obtained from barley cDNAs encoding two types of glycine-rich proteins: HvGRP2, characterized by a cytokeratin-like and a cysteine-rich domain, and HvGRP3, whose main feature was an RNA-binding domain. Expression of genes Hvgrp2 and Hvgrp3, which are present at one (or two) copies per haploid genome, was ubiquitous and gene Hvgrp3 was under light/darkness modulation. Cold treatment increased Hvgrp2 and Hvgrp3 mRNA levels. Methyl jasmonate (10 μM) switched off the two genes. Expression of Hvgrp2, but not that of Hvgrp3, was induced by ethylene treatment (100 ppm). Fungal pathogens Erysiphe graminis and Rhynchosporium secalis increased the mRNAs levels of the two genes, both in compatible and in incompatible interactions, while bacterial pathogens did not.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005712803130
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  • 8
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of a cDNA encoding an α/β-type gliadin from hexaploid wheat (Triticum aestivum) (1990)
    Springer
    Plant molecular biology 14 (1990), S. 867-868 
    Details
    ISSN: 1573-5028
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00016521
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  • 9
    Electronic Resource
    Electronic Resource
    In vivo and in vitro synthesis of CM-proteins (A-hordeins) from barley (Hordeum vulgare L.) (1983)
    Springer
    Planta 157 (1983), S. 74-80 
    Details
    ISSN: 1432-2048
    Keywords: A-hordein ; CM-proteins ; Endosperm ; Hordeum (A-hordeins) ; Protein biosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract CM-proteins from barley endosperm (CMa, CMb, CMc, CMd), which are the main components of the A-hordein fraction, are synthesized most actively 10 to 30 d after anthesis (maximum at 15–20 d). They are synthesized by membranebound polysomes as precursors of higher apparent molecular weight (13,000–21,000) than the mature proteins (12,000–16,000). The largest in vitro product (21,000) is the putative precursor of protein CMd (16,000), as it is selected with anti-CMd monospecific IgG's, and is coded by an mRNA of greater sedimentation coefficient (9 S) than those encoding the other three proteins (7.5 S). CM-proteins always appear in the soluble fraction, following different homogenization and subcellular fractionation procedures, indicating that these proteins are transferred to the soluble fraction after processing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00394543
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  • 10
    Electronic Resource
    Electronic Resource
    Two cold-inducible genes encoding lipid transfer protein LTP4 from barley show differential responses to bacterial pathogens (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 162-168 
    Details
    ISSN: 1617-4623
    Keywords: Key words Bacterial pathogens ; Barley ; Lipid transfer proteins ; Low temperature ; Promoter analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The barley genes HvLtp4.2 and HvLtp4.3 both encode the lipid transfer protein LTP4 and are less than 1 kb apart in tail-to-tail orientation. They differ in their non-encoding regions from each other and from the gene corresponding to a previously reported Ltp4 cDNA (now Ltp4.1). Southern blot analysis indicated the existence of three or more Ltp4 genes per haploid genome and showed considerable polymorphism among barley cultivars. We have ingestigated the transient expression of genes HvLtp4.2 and HvLtp4.3 following transformation by particle bombardment, using promoter fusions to the β-glucuronidase reporter sequence. In leaves, activities of the two promoters were of the same order as those of the sucrose synthase (Ss1) and cauliflower mosaic virus 35S promoters used as controls. Their expression patterns were similar, except that Ltp4.2 was more active than Ltp4.3 in endosperm, and Ltp4.3 was active in roots, while Ltp4.2 was not. The promoters of both genes were induced by low temperature, both in winter and spring barly cultivars. Northern blot analysis, using the Ltp4-specific probe, indicated that Xanthomonas campestris pv. translucens induced an increase over basal levels of Ltp4 mRNA, while Pseudomonas syringae pv. japonica caused a decrease. The Ltp4.3-Gus promoter fusion also responded in opposite ways to these two compatible bacterial pathogens, whereas the Ltp4.2-Gus construction did not respond to infection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004389670018
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