Abstract
The vectors for heterologous gene expression in S. pombe have been developed and high-level productions of several proteins have been achieved. In the case of the secretory proteins, however, few proteins have successfully been secreted. Secretory proteins must enter the secretory pathway (composed mainly of endoplasmic reticulum (ER) and Golgi apparatus accompanied with the removal of the signal sequence of each protein by a signal peptidase in the host cells for correct folding, disulfide bonds, glycosylation, etc. Some heterologous secretory proteins such as human antithrombin III,1 human gastric lipase,2 human placental alkaline phosphatase (chapter 10) and S. cerevisiae invertase3,4 can be produced extracellulary with the removal of their own signal sequence, while some signal sequences of secretory proteins are not recognized by the signal peptidase in S. pombe. The signal sequences functionable in S. pombe have not yet been exploited extensively except for the secretion signal of the killer toxin of Kluiveromyces lactis. 5 The development of convenient secretion vectors is important for the production of secretory proteins with a natural structure.
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Giga-Hama, Y. (1997). Secretion of Human Interleukin-6 Using the P-Factor Secretion Signal in Schizosaccharomyces pombe . In: Giga-Hama, Y., Kumagai, H. (eds) Foreign Gene Expression in Fission Yeast: Schizosaccharomyces pombe . Biotechnology Intelligence Unit. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-03472-9_11
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DOI: https://doi.org/10.1007/978-3-662-03472-9_11
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