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2019, DOI: 10.1111/pce.13473

BSD2 is a Rubisco‐specific assembly chaperone, forms intermediary hetero‐oligomeric complexes, and is nonlimiting to growth in tobacco

Plant, Cell & Environment

Brendon Conlan, Rosemary Birch, Celine Kelso, Sophie Holland, Amanda P. De Souza, Stephen P. Long, Jennifer L. Beck, and Spencer M. Whitney


The folding and assembly of Rubisco large and small subunits into L8S8 holoenzyme in chloroplasts involves many auxiliary factors, including the chaperone BSD2. Here we identify apparent intermediary Rubisco‐BSD2 assembly complexes in the model C3 plant tobacco. We show BSD2 and Rubisco content decrease in tandem with leaf age with approximately half of the BSD2 in young leaves (~70 nmol BSD2 protomer.m2) stably integrated in putative intermediary Rubisco complexes that account for <0.2% of the L8S8pool. RNAisilencing BSD2 production in transplastomic tobacco producing bacterial L2Rubisco had no effect on leaf photosynthesis, cell ultrastructure, or plant growth. Genetic crossing the same RNAi‐bsd2 alleles into wild‐type tobacco however impaired L8S8Rubisco production and plant growth, indicating the only critical function of BSD2 is in Rubisco biogenesis. Agrobacterium mediated transient expression of tobacco, Arabidopsis, or maize BSD2 reinstated Rubisco biogenesis in BSD2‐silenced tobacco. Overexpressing BSD2 in tobacco chloroplasts however did not alter Rubisco content, activation status, leaf photosynthesis rate, or plant growth in the field or in the glasshouse at 20°C or 35°C. Our findings indicate BSD2 functions exclusively in Rubisco biogenesis, can efficiently facilitate heterologous plant Rubisco assembly, and is produced in amounts nonlimiting to tobacco growth.

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The LongLab is supported by many public and private partnerships, including the Bill & Melinda Gates Foundation, the Foundation for Food and Agriculture Research, the UK Government's Department for International Development, the U.S. Department of Energy, and the Advanced Research Projects Agency-Energy.

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