Identification of cAMP-dependent phosphorylated proteins involved in the formation of environment-resistant resting cysts by the terrestrial ciliate Colpoda cucullus

Authors

  • Y Sogame Department of Biological Science, Faculty of Science, Kochi University, Kochi 780-8520, Japan
  • K Kojima Department of Microbiology and Immunology, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390-8621, Japan
  • T Takeshita Department of Microbiology and Immunology, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390-8621, Japan
  • E Kinoshita Department of Functional Molecular Science, Institute of Biomedical & Health Sciences, Hiroshima University, Kasumi 1-2-3, Hiroshima 734-8553, Japan
  • T Matsuoka Department of Biological Science, Faculty of Science, Kochi University, Kochi 780-8520, Japan

Keywords:

environment-resistant cyst, Colpoda, encystment, protein phosphorylation, cAMP

Abstract

In the terrestrial ciliate Colpoda cucullus, an elevation of the intracellular cAMP concentration was reported to be involved in environment-resistant resting cyst formation. In the present study, cAMP-dependently phosphorylated proteins of encystment-induced C. cucullus were isolated with Phos-tag agarose phosphate-affinity beads and subsequent SDS-PAGE. In a liquid
chromatography/tandem mass spectrometry analysis of these phosphoproteins, 27-, 37- and 43-kDa proteins (p27, p37 and p43) were identified as Rieske iron-sulfur protein, histone H4 (hyperacetylated form), and actin, respectively.

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Published

2014-06-26

Issue

Section

Research Reports