AI Article Synopsis
- The moss Physcomitrella patens has been engineered to secrete enzymes and binding proteins into its apoplast, enhancing its ability to perform biochemical reactions.
- This process employs a modular membrane anchoring system based on a specific protein (SERK) identified through bioinformatics, allowing for targeted protein functionalization.
- The system was validated by attaching a luciferase enzyme to the SERK signal peptide, demonstrating successful secretion and localization in the moss, paving the way for potential biotechnological applications.
Article Abstract
Heterologous enzymes and binding proteins were secreted by the moss Physcomitrella patens or anchored extracellularly on its cell membrane in order to functionalize the apoplast as a biochemical reaction compartment. This modular membrane anchoring system utilizes the signal peptide and the transmembrane segment of the somatic embryogenesis receptor-like kinase (SERK), which were identified in a comprehensive bioinformatic analysis of the P. patens genome. By fusing the soluble enzyme NanoLuc luciferase to the signal peptide, its secretion capability was confirmed in vivo. The membrane localization of hybrid proteins comprising the SERK signal peptide, NanoLuc or other functional modules, the SERK transmembrane anchor, and a C-terminal GFP reporter was demonstrated using fluorescence microscopy as well as site-specific proteolytic release of the extracellular enzyme domain. Our membrane anchoring system enables the expression of various functional proteins in the apoplast of P. patens, empowering this photoautotrophic organism for biotechnological applications.
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| http://dx.doi.org/10.1021/sb5000302 | DOI Listing |
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