Resistance acquisition of Thiobacillus thiooxidans upon cadmium and zinc ion addition and formation of cadmium ion-binding and zinc ion-binding proteins exhibiting metallothionein-like properties

Kazuyuki Sakamoto, Makoto Yagasaki, Kotaro Kirimura, Shoji Usami

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    15 Citations (Scopus)

    Abstract

    Through subcultivations of Thiobacillus thiooxidans WU-79A in autotrophic media in which the concentrations of Cd2+ and Zn2+ were increased successively, Cd2+-resistant (CDR) and Zn2+-resistant strains (ZNR) were obtained. The growth of WU-79A was inhibited by the addition of 25 mM Cd2+ as well as Zn2+. However, CDR and ZNR could grow without any lag phase in media containing 200 mM Cd2+ and 250 mM Zn2+, respectively. CDR and ZNR were able to grow even in media containing up to 400 mM Cd2+ and 600 mM Zn2+, respectively, although they exhibited lag phases. CDR could grow in medium containing up to 250 mM Zn2+, as could ZNR in medium containing up to 200 mM Cd2+. Cd2+-binding and Zn2+-binding proteins were isolated from CDR and ZNR, respectively, by gel filtration and ion exchange chromatography. The molecular weights of both proteins were estimated to be approximately 13,000 by gel filtration. The fact that there was no strong absorption at 280 nm of the proteins suggested that they had few aromatic amino acids. Broad absorption bands which are typical of mercaptide (metal thiolate) complexes were detected. The properties of the proteins were spectrophotometrically similar to those of metallothionein.

    Original languageEnglish
    Pages (from-to)266-273
    Number of pages8
    JournalJournal of Fermentation and Bioengineering
    Volume67
    Issue number4
    DOIs
    Publication statusPublished - 1989

    Fingerprint

    Acidithiobacillus thiooxidans
    Metallothionein
    Cadmium
    Zinc
    Carrier Proteins
    Ions
    Proteins
    Gel Chromatography
    Gels
    Aromatic Amino Acids
    Coordination Complexes
    Ion Exchange Chromatography
    Metal complexes
    Chromatography
    Carboxylic acids
    Amino acids
    Absorption spectra
    Ion exchange
    Molecular Weight
    Molecular weight

    ASJC Scopus subject areas

    • Biotechnology
    • Applied Microbiology and Biotechnology

    Cite this

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    title = "Resistance acquisition of Thiobacillus thiooxidans upon cadmium and zinc ion addition and formation of cadmium ion-binding and zinc ion-binding proteins exhibiting metallothionein-like properties",
    abstract = "Through subcultivations of Thiobacillus thiooxidans WU-79A in autotrophic media in which the concentrations of Cd2+ and Zn2+ were increased successively, Cd2+-resistant (CDR) and Zn2+-resistant strains (ZNR) were obtained. The growth of WU-79A was inhibited by the addition of 25 mM Cd2+ as well as Zn2+. However, CDR and ZNR could grow without any lag phase in media containing 200 mM Cd2+ and 250 mM Zn2+, respectively. CDR and ZNR were able to grow even in media containing up to 400 mM Cd2+ and 600 mM Zn2+, respectively, although they exhibited lag phases. CDR could grow in medium containing up to 250 mM Zn2+, as could ZNR in medium containing up to 200 mM Cd2+. Cd2+-binding and Zn2+-binding proteins were isolated from CDR and ZNR, respectively, by gel filtration and ion exchange chromatography. The molecular weights of both proteins were estimated to be approximately 13,000 by gel filtration. The fact that there was no strong absorption at 280 nm of the proteins suggested that they had few aromatic amino acids. Broad absorption bands which are typical of mercaptide (metal thiolate) complexes were detected. The properties of the proteins were spectrophotometrically similar to those of metallothionein.",
    author = "Kazuyuki Sakamoto and Makoto Yagasaki and Kotaro Kirimura and Shoji Usami",
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    T1 - Resistance acquisition of Thiobacillus thiooxidans upon cadmium and zinc ion addition and formation of cadmium ion-binding and zinc ion-binding proteins exhibiting metallothionein-like properties

    AU - Sakamoto, Kazuyuki

    AU - Yagasaki, Makoto

    AU - Kirimura, Kotaro

    AU - Usami, Shoji

    PY - 1989

    Y1 - 1989

    N2 - Through subcultivations of Thiobacillus thiooxidans WU-79A in autotrophic media in which the concentrations of Cd2+ and Zn2+ were increased successively, Cd2+-resistant (CDR) and Zn2+-resistant strains (ZNR) were obtained. The growth of WU-79A was inhibited by the addition of 25 mM Cd2+ as well as Zn2+. However, CDR and ZNR could grow without any lag phase in media containing 200 mM Cd2+ and 250 mM Zn2+, respectively. CDR and ZNR were able to grow even in media containing up to 400 mM Cd2+ and 600 mM Zn2+, respectively, although they exhibited lag phases. CDR could grow in medium containing up to 250 mM Zn2+, as could ZNR in medium containing up to 200 mM Cd2+. Cd2+-binding and Zn2+-binding proteins were isolated from CDR and ZNR, respectively, by gel filtration and ion exchange chromatography. The molecular weights of both proteins were estimated to be approximately 13,000 by gel filtration. The fact that there was no strong absorption at 280 nm of the proteins suggested that they had few aromatic amino acids. Broad absorption bands which are typical of mercaptide (metal thiolate) complexes were detected. The properties of the proteins were spectrophotometrically similar to those of metallothionein.

    AB - Through subcultivations of Thiobacillus thiooxidans WU-79A in autotrophic media in which the concentrations of Cd2+ and Zn2+ were increased successively, Cd2+-resistant (CDR) and Zn2+-resistant strains (ZNR) were obtained. The growth of WU-79A was inhibited by the addition of 25 mM Cd2+ as well as Zn2+. However, CDR and ZNR could grow without any lag phase in media containing 200 mM Cd2+ and 250 mM Zn2+, respectively. CDR and ZNR were able to grow even in media containing up to 400 mM Cd2+ and 600 mM Zn2+, respectively, although they exhibited lag phases. CDR could grow in medium containing up to 250 mM Zn2+, as could ZNR in medium containing up to 200 mM Cd2+. Cd2+-binding and Zn2+-binding proteins were isolated from CDR and ZNR, respectively, by gel filtration and ion exchange chromatography. The molecular weights of both proteins were estimated to be approximately 13,000 by gel filtration. The fact that there was no strong absorption at 280 nm of the proteins suggested that they had few aromatic amino acids. Broad absorption bands which are typical of mercaptide (metal thiolate) complexes were detected. The properties of the proteins were spectrophotometrically similar to those of metallothionein.

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