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Soybean peroxidase propeptides are functional signal peptides and increase the yield of a foreign protein

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Abstract

Elements that contribute to the high, stable yield of soybean peroxidase (SBP) in soybean seed coats can be exploited in the development of this tissue as a protein production platform. SBP contains an N-terminal and a C-terminal propeptide that are predicted to direct vacuolar targeting; this may be one factor that contributes to its high yield and stability. We characterized the function of the SBP propeptides and investigated their ability to increase the yield of a foreign protein in a heterologous plant system. SBP propeptides are functional signal peptides capable of directing vacuolar transport in Arabidopsis. The use of these propeptides as well as an endoplasmic reticulum (ER)-retention signal to direct a foreign protein to the apoplast, ER, or vacuole can significantly increase yield and will therefore be useful for the development of the seed coat as a protein production platform. We also demonstrate that growth conditions may have a significant impact on the yield of a foreign protein and that this may be subcellular compartment-specific.

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Acknowledgments

The authors would like to thank Dr. Federica Brandizzi for help with confocal microscopy and vector design, Mr. Ann-fook Yang and Ms. Denise Chabot for support at the confocal facility, AAFC, Ottawa, Dr. David Currie and Martha Mullally for help with statistical analyses, Cathy Sun for assistance with the peroxidase enzyme assays, and Alex Molnar for graphic design. The plasmid pETSBP was kindly provided by Drs K. Welinder and K. Lehmann Nielsen. This research was funded in part by a Strategic Grant from the Natural Sciences and Engineering Research Council of Canada. The authors declare that they have no conflict of interest.

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Correspondence to Douglas A. Johnson.

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Communicated by P. Kumar.

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Schnell, J.A., Han, S., Miki, B.L. et al. Soybean peroxidase propeptides are functional signal peptides and increase the yield of a foreign protein. Plant Cell Rep 29, 987–996 (2010). https://doi.org/10.1007/s00299-010-0884-y

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  • DOI: https://doi.org/10.1007/s00299-010-0884-y

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