<scp>EF</scp>‐1α and Mitochondrial <scp>ATP</scp> Synthase β Chain: Alteration of their Expression in Encystment‐Induced <i>Colpoda cucullus</i>
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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>Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis of the total proteins contained in encystment‐induced <jats:italic>Colpoda cucullus</jats:italic> showed that a 50‐<jats:styled-content style="fixed-case">kD</jats:styled-content>a protein (p50) disappeared, whereas the expression of a 49‐<jats:styled-content style="fixed-case">kD</jats:styled-content>a protein (p49) was enhanced in early phase of morphogenetic transformation into the resting cyst (i.e. 2–5 h after the onset of encystment induction). Puromycin or actinomycin D inhibited the alteration in the expression of p50 and p49 by the induction of encystment. These results suggest that the encystment‐specific alteration in expression of these proteins is performed by a transcriptional regulation. Liquid chromatography tandem mass spectrometry analysis revealed that p50 is mitochondrial <jats:styled-content style="fixed-case">ATP</jats:styled-content> synthase β chains, and that p49 is elongation factor 1α.</jats:p>
収録刊行物
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- Journal of Eukaryotic Microbiology
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Journal of Eukaryotic Microbiology 59 (4), 401-406, 2012-06-18
Wiley
