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  • 1995-1999  (2)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Phytopathology 37 (1999), S. 447-471 
    ISSN: 0066-4286
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Biology
    Notes: Abstract Melanins are darkly pigmented polymers that protect organisms against environmental stress. Even when not directly involved in pathogenesis, fungal melanin is likely required by melanizing phytopathogens for survival in the environment. However, some phytopathogenic fungi that produce melanized appressoria for host invasion require appressorial melanogenesis for pathogenicity. Much less is known about the role melanins play in pathogenesis during infection by other phytopathogens that do not rely on appressoria for host penetration. Here we focus on one such phytopathogenic fungus, Gaeumannomyces graminis var. tritici, the etiologic agent of the devastating root disease of cereals, take-all. This fungus is lightly pigmented in culture, but requires melanin biosynthesis for pathogenesis, perhaps to produce melanized, ectotrophic macrohyphae on roots. However, the constitutively melanized, asexual Phialophora anamorph of G. graminis var. tritici is nonpathogenic. In addition, melanization of G. graminis var. graminis is not required to produce root disease on its rice host. Explanations for these apparent contradictions are suggested, as are other functions for the melanins of phytopathogenic fungi.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 177 (1999), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A ptsH homologue of Streptomyces coelicolor A3(2) was identified in the emerging genome sequence, cloned in Escherichia coli and the S. coelicolor HPr over-produced and purified. The protein was phosphorylated in vitro in a phosphoenolpyruvate (PEP)-dependent manner by purified enzyme I (EI) from Bacillus subtilis, and much less efficiently in an ATP-dependent manner by purified HPr kinase, also from B. subtilis. There was no indication of ATP-dependent phosphorylation of the purified protein by cell extracts of either S. coelicolor or Streptomyces lividans. Deletion of the ptsH homologue from the S. coelicolor and S. lividans chromosomes had no effect on growth when fructose was supplied as sole carbon source, and in S. coelicolor it had no effect on glucose repression of agarase and galactokinase synthesis, suggesting that the HPr encoded by this gene does not play an essential role in fructose transport nor a general role in carbon catabolite repression.
    Type of Medium: Electronic Resource
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