期刊
FEMS MICROBIOLOGY LETTERS
卷 331, 期 2, 页码 128-135出版社
WILEY-BLACKWELL
DOI: 10.1111/j.1574-6968.2012.02560.x
关键词
Colpoda; encystment; phosphorylation; Phos-tag; ribosomal P0 protein; ribosomal S5 protein
类别
资金
- Grants-in-Aid for Scientific Research [22570214, 22590037] Funding Source: KAKEN
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.
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