Identification of Differentially Expressed Water‐insoluble Proteins in the Encystment Process of <i>Colpoda cucullus</i> by Two‐dimensional Electrophoresis and <scp>LC</scp>‐<scp>MS</scp>/<scp>MS</scp> Analysis
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- Yoichiro Sogame
- Department of Biological Science Faculty of Science Kochi University Kochi 780‐8520 Japan
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- Katsuhiko Kojima
- Department of Microbiology and Immunology Shinshu University School of Medicine 3‐1‐1 Asahi Matsumoto Nagano 390‐8621 Japan
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- Toshikazu Takeshita
- Department of Microbiology and Immunology Shinshu University School of Medicine 3‐1‐1 Asahi Matsumoto Nagano 390‐8621 Japan
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- Eiji Kinoshita
- Department of Functional Molecular Science Graduate School of Biomedical Sciences Hiroshima University Kasumi 1‐2‐3 Hiroshima 734‐8553 Japan
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- Tatsuomi Matsuoka
- Department of Biological Science Faculty of Science Kochi University Kochi 780‐8520 Japan
説明
<jats:title>ABSTRACT</jats:title><jats:p>In the encystment process of the ciliate protist <jats:italic>Colpoda cucullus</jats:italic>, we observed that the cell total protein abundance was reduced at 12 h–1 d after the onset of encystment induction subsequent to the reduction in <jats:styled-content style="fixed-case">mRNA</jats:styled-content> abundance. We analyzed the alteration of the expression levels of water‐insoluble proteins by two‐dimensional polyacrylamide gel electrophoresis using polyoxyethylene (20) sorbitan monooleate (Tween‐80), and we identified proteins whose expression levels were altered in the encystment process by a liquid chromatography tandem mass spectrometry analysis. The expression level of a 60‐<jats:styled-content style="fixed-case">kD</jats:styled-content>a protein (p60; heat shock protein 60) was temporarily enhanced and that of a 55‐<jats:styled-content style="fixed-case">kD</jats:styled-content>a protein (p55; actin) and a 49‐<jats:styled-content style="fixed-case">kD</jats:styled-content>a protein (p49; actin) was enhanced in the <jats:italic>Colpoda</jats:italic> encystment process. In mature cysts, the expression level of p55 and p49 tended to be reduced, whereas the expression level of a 50‐<jats:styled-content style="fixed-case">kD</jats:styled-content>a protein (p50d; α‐tubulin), a 25‐<jats:styled-content style="fixed-case">kD</jats:styled-content>a protein (p25; α‐tubulin) and a 52‐<jats:styled-content style="fixed-case">kD</jats:styled-content>a protein (p52c; β‐tubulin) was enhanced.</jats:p>
収録刊行物
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- Journal of Eukaryotic Microbiology
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Journal of Eukaryotic Microbiology 61 (1), 51-60, 2013-11-12
Wiley
