期刊
PLANT JOURNAL
卷 79, 期 1, 页码 1-12出版社
WILEY
DOI: 10.1111/tpj.12536
关键词
beta-carboxysome; synthetic biology; photosynthesis; CO2 concentration mechanism; chloroplast engineering; bacterial microcompartment; Nicotiana benthamiana
资金
- National Science Foundation [EF-1105584]
- Biotechnology and Biological Sciences Research Council [BB/I024488/1]
- National Institute of General Medical Sciences of the National Institutes of Health [F32GM103019]
- Biotechnology and Biological Sciences Research Council [BBS/E/C/00005202, BB/I024488/1] Funding Source: researchfish
- Emerging Frontiers
- Direct For Biological Sciences [1105584] Funding Source: National Science Foundation
- BBSRC [BBS/E/C/00005202, BB/I024488/1] Funding Source: UKRI
The photosynthetic efficiency of C3 plants suffers from the reaction of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) with O-2 instead of CO2, leading to the costly process of photorespiration. Increasing the concentration of CO2 around Rubisco is a strategy used by photosynthetic prokaryotes such as cyanobacteria for more efficient incorporation of inorganic carbon. Engineering the cyanobacterial CO2-concentrating mechanism, the carboxysome, into chloroplasts is an approach to enhance photosynthesis or to compartmentalize other biochemical reactions to confer new capabilities on transgenic plants. We have chosen to explore the possibility of producing beta-carboxysomes from Synechococcus elongatus PCC7942, a model freshwater cyanobacterium. Using the agroinfiltration technique, we have transiently expressed multiple beta-carboxysomal proteins (CcmK2, CcmM, CcmL, CcmO and CcmN) in Nicotiana benthamiana with fusions that target these proteins into chloroplasts, and that provide fluorescent labels for visualizing the resultant structures. By confocal and electron microscopic analysis, we have observed that the shell proteins of the b-carboxysome are able to assemble in plant chloroplasts into highly organized assemblies resembling empty microcompartments. We demonstrate that a foreign protein can be targeted with a 17-amino-acid CcmN peptide to the shell proteins inside chloroplasts. Our experiments establish the feasibility of introducing carboxysomes into chloroplasts for the potential compartmentalization of Rubisco or other proteins.
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