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1 July 2001 Purification of GVBD-Inducing Protein from the Ciliate Tetrahymena thermophila
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Abstract

Germinal-vesicle-breakdown (GVBD) was induced if a 132,000-g supernatant of Tetrahymena thermophila homogenates was injected into Xenopus oocytes. Using this induction of GVBD as a bioassay system, a GVBD-inducing substance was purified from the Tetrahymena by ultra-filtration, liquid chromatography, and electroelution from a band on native-PAGE gel. Proteins eluted from the single band on the native-PAGE gel induced GVBD in the absence of oocyte protein synthesis. This band resolved into two bands on SDS-PAGE: 60 and 112 kDa. The 60 kDa protein was the active fraction inducing GVBD. Immunoprecipitation of the 60 kDa protein prevented the GVBD-inducing activity, supporting the conclusion that the 60 kDa protein is the GVBD-inducing substance. An immunoblot with anti-60 kDa monoclonal antibody and PSTAIR antibody showed that p13suc1-beads could remove cdc2 homologues from T. thermophila supernatant but could not remove the GVBD-inducing activity. The 60-kDa protein appeared at the same time as micronuclear division and disappeared at the beginning of the macronuclear division during synchronous cell division. The cyclic appearance of the 60-kDa protein in the T. thermophila cell cycle suggests that this protein has a cell cycle function.

MANABU SUGII and MASAHIRO FUJISHIMA "Purification of GVBD-Inducing Protein from the Ciliate Tetrahymena thermophila," The Journal of Eukaryotic Microbiology 48(4), 414-424, (1 July 2001). https://doi.org/10.1111/j.1550-7408.2001.tb00174.x
Received: 11 October 2000; Accepted: 27 February 2001; Published: 1 July 2001
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