EF-1α and mitochondrial ATP synthase β chain: alteration of their expression in encystment-induced Colpoda cucullus.
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the total proteins contained in encystment-induced Colpoda cucullus showed that a 50-kDa protein (p50) disappeared, whereas the expression of a 49-kDa 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 ATP synthase β chains, and that p49 is elongation factor 1α.
Department of Biological Science, Faculty of Science, Kochi University, Kochi, Japan.
Yoichiro
Y
Sogame
Katsuhiko
K
Kojima
Toshikazu
T
Takeshita
Eiji
E
Kinoshita
Tatsuomi
T
Matsuoka
D002853:Chromatography, Liquid; D016798:Ciliophora / Q000201:enzymology / Q000235:genetics / Q000254:growth & development*; D004591:Electrophoresis, Polyacrylamide Gel; D005786:Gene Expression Regulation; D025261:Mitochondrial Proton-Translocating ATPases / Q000096:biosynthesis* / Q000737:chemistry; D008970:Molecular Weight; D020648:Peptide Elongation Factor 1 / Q000096:biosynthesis* / Q000737:chemistry; D020543:Proteome / Q000032:analysis; D015800:Protozoan Proteins / Q000032:analysis; D053719:Tandem Mass Spectrometry
D020648:Peptide Elongation Factor 1; D020543:Proteome; D015800:Protozoan Proteins; D025261:Mitochondrial Proton-Translocating ATPases