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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Plant pathology 54 (2005), S. 0 
    ISSN: 1365-3059
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: The effect of small temperature differentials (16 vs. 20°C) on the pathogenicity of deoxynivalenol producing single isolates of Fusarium culmorum and F. graminearum and on the fusarium head blight (FHB) response of eight wheat cultivars was examined. Fusarium culmorum inoculation caused greater visual disease symptoms at 20°C than at 16°C, both overall and on an individual cultivar basis (overall AUDPC = 13·5 and 9·6, respectively) (P 〈 0·05). In contrast, F. graminearum inoculation caused greater overall visual disease symptoms at 16°C than at 20°C, both overall and at the individual cultivar level (overall AUDPC = 12·8 and 10·9, respectively) (P 〈 0·05). Results showed both F. culmorum and F. graminearum inoculations caused a greater loss in yield at 20°C (54·3 and 46·9% relative 1000-grain weight, respectively) compared with 16°C (73·3 and 66·9% relative 1000-grain weight, respectively) (P 〈 0·05). Fusarium culmorum-inoculated heads contained similar amounts of fungal DNA at both 16 and 20°C (1·9 and 1·7 ng mg−1 of plant material, respectively) (not significant), while for F. graminearum inoculation, plants contained higher amounts of fungal DNA at 20°C (2·0 and 1·0 ng mg−1 of plant material, respectively) (P 〈 0·05). Overall, there was a significant negative correlation between AUDPC and percentage relative 1000-grain weight at both 16 and 20°C (r =−0·693 and −0·794, respectively, P 〈 0·01).
    Type of Medium: Electronic Resource
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  • 2
    Publication Date: 2012-12-22
    Description: Every known SWI/SNF chromatin-remodeling complex incorporates an ARID DNA binding domain-containing subunit. Despite being a ubiquitous component of the complex, physiological roles for this domain remain undefined. Here, we show that disruption of ARID1a-DNA binding in mice results in embryonic lethality, with mutant embryos manifesting prominent defects in the heart and extraembryonic vasculature. The DNA binding-defective mutant ARID1a subunit is stably expressed and capable of assembling into a SWI/SNF complex with core catalytic properties, but nucleosome substrate binding and promoter occupancy by ARID1a-containing SWI/SNF complexes (BAF-A) are impaired. Depletion of ARID domain-dependent, BAF-A associations at THROMBOSPONDIN 1 ( THBS1 ) led to the concomitant upregulation of this SWI/SNF target gene. Using a THBS1 promoter-reporter gene, we further show that BAF-A directly regulates THBS1 promoter activity in an ARID domain-dependent manner. Our data not only demonstrate that ARID1a-DNA interactions are physiologically relevant in higher eukaryotes but also indicate that these interactions facilitate SWI/SNF binding to target sites in vivo . These findings support the model wherein cooperative interactions among intrinsic subunit-chromatin interaction domains and sequence-specific transcription factors drive SWI/SNF recruitment.
    Print ISSN: 0270-7306
    Electronic ISSN: 1098-5549
    Topics: Biology , Medicine
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