Protein phosphorylation in encystment-induced Colpoda cucullus: localization and identification of phosphoproteins
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- Yoichiro Sogame
- Institute of Biological Science; Faculty of Science; Kochi University; Kochi; Japan
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- Katsuhiko Kojima
- Department of Microbiology and Immunology; Shinshu University School of Medicine; Nagano; Japan
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- Toshikazu Takeshita
- Department of Microbiology and Immunology; Shinshu University School of Medicine; Nagano; Japan
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- Shigeki Fujiwara
- Department of Applied Science; Faculty of Science; Kochi University; Kochi; Japan
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- Seiji Miyata
- Department of Applied Biology; Kyoto Institute of Technology; Kyoto; Japan
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- Eiji Kinoshita
- Department of Functional Molecular Science; Graduate School of Biomedical Sciences; Hiroshima University; Hiroshima; Japan
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- Tatsuomi Matsuoka
- Institute of Biological Science; Faculty of Science; Kochi University; Kochi; Japan
説明
In Colpoda cucullus, the morphogenetic transformation was preceded by an enhancement of the in vivo protein phosphorylation level. Immunofluorescence microscopy using antiphosphoserine antibody showed that these phosphorylated proteins were localized in the macronucleus and other cytoplasmic regions. Biotinylated Phos-tag/ECL assays of isolated macronuclei showed that a 33-kDa protein (p33) was localized within them. The p33 obtained from isolated macronuclei was tentatively identified as ribosomal P0 protein by LC-MS/MS analysis. In addition, among the encystment-specific phosphoproteins obtained by phosphate-affinity chromatography, the 29-, 31-, and 33-kDa proteins (p29, p31, and p33) were tentatively identified as ribosomal P0 protein, whereas the 24-kDa phosphoprotein (p24) was tentatively identified as ribosomal S5 protein.
収録刊行物
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- FEMS Microbiology Letters
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FEMS Microbiology Letters 331 (2), 128-135, 2012-04-20
Oxford University Press (OUP)
