Soil Microorganisms
Online ISSN : 2189-6518
Print ISSN : 0912-2184
ISSN-L : 0912-2184
Volume 37
Displaying 1-7 of 7 articles from this issue
  • Yutaka MORI
    Article type: Article
    1991 Volume 37 Pages 1-8
    Published: February 01, 1991
    Released on J-STAGE: May 31, 2017
    JOURNAL FREE ACCESS
    A thermophilic, anaerobic bacterium, Clostridium thermocellum, produces the enzyme complexes termed cellulosome (2-3.5×10^6Da), and polycellulosome (50-80×10^6 Da), that differ substantially from those of the better characterized cellulases from fungi. The complexes exhibit enzymatic activities for the hydrolysis of crystalline cellulose, carboxymethylcellulose, cellobiose, and xylan, which account for most of the cellulolytic activity of the bacterium. The cellulosome is assumed to be composed of sets of polypeptides arranged in ordered chainlike arrays with a definite orientation. It contains Ca, Zn, and carbohydrates. Calcium is essential for the hydrolysis of crystalline cellulose. The cellulosome, together with a gluelike substance also produced by the bacterium, is considered to be responsible for the adherence of the bacterium to cellulose. The binding of the cellulosome to cellulose is facilitated by a yellow affinity substance (YAS) which is produced by the bacterium after contact is made with cellulose. YAS is a low molecular, hydrophobic, carotenoid-like substance. Cellobiose and short-chain oligosaccharides produced by the cellulosome are metabolized by β-glucosidase or cellobiose phosphorylase in the periplasmic space.
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  • Kimiko YABE
    Article type: Article
    1991 Volume 37 Pages 9-14
    Published: February 01, 1991
    Released on J-STAGE: May 31, 2017
    JOURNAL FREE ACCESS
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  • Takashi TSUGE
    Article type: Article
    1991 Volume 37 Pages 15-25
    Published: February 01, 1991
    Released on J-STAGE: May 31, 2017
    JOURNAL FREE ACCESS
    In the plant diseases caused by the fungus Alternaria, there are at least seven known host-parasite combinations, in which host-selective toxins (HSTs) are responsible for the host-selective pathogenicity. These toxins are highly toxic to the host plants of the producing fungi while non-host plants are tolerant. The HST producers are considered to be distinct pathotypes of the species of Alternaria alternate. All the known Alternaria HSTs could be detected from the spore-germination fluids of each pathogen, suggesting that the participation of HST at the early infection process, resulted in the successful penetration of the pathogen into the host cells. The chemical structure of six HSTs was determined, and the primary action sites of the HSTs in the host cells were identified based on physiological and cytological studies. The analysis of the structure-toxicity relationships provided a chemical basis for the host-selective activity of HSTs and suggested the presence of potential receptor sites for HST in the host cells. For the analysis of the genetic regulation of HST production of A. alternata pathogens, studies on pathways and genes for HST synthesis have been initiated, especially by using the A. alternate Japanese pear pathotype (AK-toxin producer). Epoxy-decatrienoic acid was found to be an important intermediate for AK-toxin production. Gene manipulation techniques, including genetic transformation and direct gene isolation by complementation of mutants, were developed for A. alternate.
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  • Yoshimasa TANAKA
    Article type: Article
    1991 Volume 37 Pages 27-36
    Published: February 01, 1991
    Released on J-STAGE: May 31, 2017
    JOURNAL FREE ACCESS
  • Osami YAGI, Hiroo UCHIYAMA
    Article type: Article
    1991 Volume 37 Pages 37-44
    Published: February 01, 1991
    Released on J-STAGE: May 31, 2017
    JOURNAL FREE ACCESS
  • [in Japanese]
    Article type: Article
    1991 Volume 37 Pages 45-
    Published: February 01, 1991
    Released on J-STAGE: May 31, 2017
    JOURNAL FREE ACCESS
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  • [in Japanese]
    Article type: Article
    1991 Volume 37 Pages 46-
    Published: February 01, 1991
    Released on J-STAGE: May 31, 2017
    JOURNAL FREE ACCESS
    Download PDF (176K)
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