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Processing of the Proteins Encoded by the Saccharomyces Retrotransposon Ty5

出版	Iowa State University, 2000
URL	http://books.google.com.hk/books?id=W6hyNwAACAAJ&hl=&source=gbs_api

註釋A mutation generated in the predicted active site of the Ty5-encoded protease is transpositionally inactive, and a single polyprotein is observed (p18OPoly). This indicates that the Ty5 protease is responsible for polyprotein processing. We followed proteolytic processing during a time course after induction of Ty5 transcription. As the culture approached stationary phase, the abundance of p37GAG reduced significantly until no longer detected. This suggests that cell culture conditions trigger either preferential degradation of p37GAG or processing to the p27GAG form. The change in abundance of p37GAG roughly corresponds to an approximately 2-fold increase in transposition. These changes in protein processing and the increase in transposition are similar to what has been observed previously for the Tf1 retrotransposon of Schizosaccharomyces pombe, which also encodes GAG and POL on a single open reading frame. For Tf1, the changes in protein abundance were considered a mechanism by which GAG/POL stoichiometry is regulated. It remains to be determined if this is the case for Ty5.