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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 41 (1985), S. 348-350 
    ISSN: 1420-9071
    Keywords: Chlamydocin ; HC-toxin ; phytotoxin ; cytostatic agent
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Chlamydocin, a potent cytostatic agent against cultured mammalian cells, and HC-toxin, a host-specific phytotoxin, are cyclic tetrapeptides containing the same epoxide α-amino acid. We show here that these compounds have reciprocal biological activity; HC-toxin is cytostatic against cultured mastocytoma cells, and chlamydocin has host-specific toxin activity against maize. Chlamydocin and another related cyclic peptide, Cyl-2, are less host-specific than HC-toxin because maize tolerant to HC-toxin is more sensitive to chlamydocin and Cyl-2.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Phytopathology 31 (1993), S. 275-303 
    ISSN: 0066-4286
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Biology
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1617-4623
    Keywords: Key wordsCochliobolus carbonum ; HC-toxin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract HC-toxin is an epoxide-containing cyclic tetrapeptide that is a critical virulence determinant in the pathogenic interaction between the filamentous fungus Cochliobolus carbonum and maize. HC-toxin exerts a potent cytostatic effect on plant and animal cells by inhibiting histone deacetylase. The biosynthesis of HC-toxin by C. carbonum is controlled by a complex genetic locus, TOX2, that contains multiple, duplicated copies of genes encoding export and biosynthetic enzymes. A new gene in the TOX2 complex, TOXE, has now been isolated. Mutation of TOXE by targeted gene disruption has no effect on growth and sporulation but abolishes HC-toxin production and pathogenicity. TOXE is required for the expression of three genes with a known or putative role in HC-toxin production, but is not required for expression of HTS1, which encodes the large, multifunctional peptide synthetase that is the central enzyme in HC-toxin biosynthesis. At its N-terminus, TOXEp has a bZIP basic DNA binding domain, but it does not contain any discernible leucine zipper or helix-loop-helix. At its carboxy terminus, TOXEp contains four ankyrin repeats. In having these two common regulatory motifs in a single polypeptide, TOXEp appears to represent a novel class of regulatory protein. TOXE is present only in HC-toxin-producing (Tox2+) isolates of C. carbonum. Most Tox2+ isolates have two copies; in strain SB111, one copy of TOXE is on the same 3.5-Mb chromosome that contains all of the other genes known to be involved in HC-toxin biosynthesis, and the second copy of TOXE is on a 0.7-Mb chromosome.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 41 (1985), S. 1370-1374 
    ISSN: 1420-9071
    Keywords: Cochliobolus victoriae ; Helminthosporium ; Bipolaris ; Avena
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The host-selective phytotoxin victorin, produced by the fungusCochliobolus victoriae, was found to be at least partially peptidic in nature, and did not contain victoxinine. The exact mass of the M-H ion was measured by FABMS as 795.1877. Derivatives of three major acid hydrolysis products were isolated. The structures of the corresponding amino acids were assigned as 2S,3R-3-hydroxyleucine, 5,5-dichloroleucine, and 3-hydroxylysine. A into victorin by the fungus in vivo.
    Type of Medium: Electronic Resource
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