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  • Articles  (2)
  • Cytochrome c 1 heme lyase  (1)
  • Ectomycorrhiza  (1)
  • Deutschland
  • Springer  (2)
  • Cambridge University Press
  • ZBW - Deutsche Zentralbibliothek für Wirtschaftswissenschaften, Leibniz-Informationszentrum Wirtschaft Kiel, Hamburg
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  • Articles  (2)
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  • Springer  (2)
  • Cambridge University Press
  • ZBW - Deutsche Zentralbibliothek für Wirtschaftswissenschaften, Leibniz-Informationszentrum Wirtschaft Kiel, Hamburg
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  • 1
    Electronic Resource
    Electronic Resource
    Expression of the Saccharomyces cerevisiae CYT2 gene, encoding cytochrome c1 heme lyase (1994)
    Springer
    Current genetics 25 (1994), S. 291-298 
    Details
    ISSN: 1432-0983
    Keywords: Cytochrome c 1 ; Cytochrome c 1 heme lyase ; GRF2p ; Glucose repression ; HAPp ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In this paper we examine the expression of the Saccharomyces cerevisiae CYT2 gene, which encodes cytochrome c 1 heme lyase. This enzyme is required for covalent attachment of heme to apocytochrome c 1, a subunit of the mitochondrial respiratory chain. Transcription of the 1-kb CYT2 mRNA initiates at four prominent sites at a distance of 52–225 bp in front of the AUG start codon. The level of CYT2 mRNA is not influenced by the presence or absence of oxygen or of heme, but it is subject to carbonsource control. The concentration of the CYT2 mRNA is significantly reduced in glucose-grown cells as compared to cells grown under non-repressing conditions. Neither the HAPp activator proteins nor MIG1p, a repressor protein involved in glucose repression, seem to mediate this effect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351480
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  • 2
    Electronic Resource
    Electronic Resource
    Rapid reactions of spruce cells to elicitors released from the ectomycorrhizal fungus Hebeloma crustuliniforme, and inactivation of these elicitors by extracellular spruce cell enzymes (1996)
    Springer
    Planta 198 (1996), S. 118-126 
    Details
    ISSN: 1432-2048
    Keywords: Ectomycorrhiza ; Elicitor inactivation ; Elicitor-induced reaction ; Hebeloma — Picea cells ; Signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Elicitors released from hyphae or cell walls of the ectomycorrhizal fungus Hebeloma crustuliniforme (Bull. ex Fries.) Quél. induced in suspension-cultured cells of Picea abies (L.) Karst. a set of fast reactions: (i) an immediate efflux of Cl− into the medium, followed by a K+ efflux; (ii) an influx of Ca2+ (measured as accumulation of 45Ca2+ in the cells); (iii) a phosphorylation of a 63-kDa protein and dephosphorylation of a 65-kDa protein (detectable by 4 min after elicitor application); (iv) an alkalinization of the medium, and (v) a transient synthesis of H2O2. The removal of extracellular Ca2+ by EGTA delayed the elicitor-induced alkalinization. A further reduction of this response could be achieved by TMB-8 an inhibitor of Ca2+ release from intracellular stores. Moreover, the inhibition of protein kinase activity by staurosporine prevented the extracellular alkalinization completely. However, the effectiveness of the elicitors in inducing the extracellular alkalinization was strongly impaired by constitutively secreted enzymes of spruce cells which cleaved the elicitors to inactive fragments. It is suggested that in ectomycorrhizae the efficacy of elicitors released from fungal cell walls is controlled by apoplastic enzymes of the host; the plant itself is able to reduce the activity of fungal elicitors on their way through the plant cell wall. But those elicitors which finally reach the plasma membrane of host cells induce reactions that are similar to the early defense reactions in plant-pathogen interactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00197594
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    Paper (German National Licenses)
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