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β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts

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β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts. / Lin, Myat T.; Occhialini, Alessandro; Andralojc, P. John; Devonshire, Jean; Hines, Kevin M.; Parry, Martin A. J.; Hanson, Maureen R.

In: Plant Journal, Vol. 79, No. 1, 01.2014, p. 1-12.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Lin, MT, Occhialini, A, Andralojc, PJ, Devonshire, J, Hines, KM, Parry, MAJ & Hanson, MR 2014, 'β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts', Plant Journal, vol. 79, no. 1, pp. 1-12. https://doi.org/10.1111/tpj.12536

APA

Lin, M. T., Occhialini, A., Andralojc, P. J., Devonshire, J., Hines, K. M., Parry, M. A. J., & Hanson, M. R. (2014). β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts. Plant Journal, 79(1), 1-12. https://doi.org/10.1111/tpj.12536

Vancouver

Lin MT, Occhialini A, Andralojc PJ, Devonshire J, Hines KM, Parry MAJ et al. β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts. Plant Journal. 2014 Jan;79(1):1-12. https://doi.org/10.1111/tpj.12536

Author

Lin, Myat T. ; Occhialini, Alessandro ; Andralojc, P. John ; Devonshire, Jean ; Hines, Kevin M. ; Parry, Martin A. J. ; Hanson, Maureen R. / β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts. In: Plant Journal. 2014 ; Vol. 79, No. 1. pp. 1-12.

Bibtex

@article{a93a4407d99544a19acf3eaff90205f1,
title = "β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts",
abstract = "The photosynthetic efficiency of C3 plants suffers from the reaction of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) with O2 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 CO 2-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 β-carboxysomes from Synechococcus elongatus PCC7942, a model freshwater cyanobacterium. Using the agroinfiltration technique, we have transiently expressed multiple β-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 β-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. ",
keywords = "bacterial microcompartment, chloroplast engineering, Nicotiana benthamiana, photosynthesis, synthetic biology, β-carboxysome",
author = "Lin, {Myat T.} and Alessandro Occhialini and Andralojc, {P. John} and Jean Devonshire and Hines, {Kevin M.} and Parry, {Martin A. J.} and Hanson, {Maureen R.}",
year = "2014",
month = jan,
doi = "10.1111/tpj.12536",
language = "English",
volume = "79",
pages = "1--12",
journal = "The Plant Journal",
issn = "0960-7412",
publisher = "Blackwell Publishing Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts

AU - Lin, Myat T.

AU - Occhialini, Alessandro

AU - Andralojc, P. John

AU - Devonshire, Jean

AU - Hines, Kevin M.

AU - Parry, Martin A. J.

AU - Hanson, Maureen R.

PY - 2014/1

Y1 - 2014/1

N2 - The photosynthetic efficiency of C3 plants suffers from the reaction of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) with O2 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 CO 2-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 β-carboxysomes from Synechococcus elongatus PCC7942, a model freshwater cyanobacterium. Using the agroinfiltration technique, we have transiently expressed multiple β-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 β-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.

AB - The photosynthetic efficiency of C3 plants suffers from the reaction of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) with O2 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 CO 2-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 β-carboxysomes from Synechococcus elongatus PCC7942, a model freshwater cyanobacterium. Using the agroinfiltration technique, we have transiently expressed multiple β-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 β-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.

KW - bacterial microcompartment

KW - chloroplast engineering

KW - Nicotiana benthamiana

KW - photosynthesis

KW - synthetic biology

KW - β-carboxysome

U2 - 10.1111/tpj.12536

DO - 10.1111/tpj.12536

M3 - Journal article

AN - SCOPUS:84903317602

VL - 79

SP - 1

EP - 12

JO - The Plant Journal

JF - The Plant Journal

SN - 0960-7412

IS - 1

ER -