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

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

Research output: Contribution to journalArticle

Abstract

The folding and assembly of Rubisco large and small subunits into L 8 S 8 holoenzyme in chloroplasts involves many auxiliary factors, including the chaperone BSD2. Here we identify apparent intermediary Rubisco-BSD2 assembly complexes in the model C 3 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.m 2 ) stably integrated in putative intermediary Rubisco complexes that account for <0.2% of the L 8 S 8 pool. RNAi-silencing BSD2 production in transplastomic tobacco producing bacterial L 2 Rubisco had no effect on leaf photosynthesis, cell ultrastructure, or plant growth. Genetic crossing the same RNAi-bsd2 alleles into wild-type tobacco however impaired L 8 S 8 Rubisco 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.

Original languageEnglish (US)
Pages (from-to)1287-1301
Number of pages15
JournalPlant Cell and Environment
Volume42
Issue number4
DOIs
StatePublished - Apr 2019

Fingerprint

Ribulose-Bisphosphate Carboxylase
ribulose-bisphosphate carboxylase
Tobacco
tobacco
Growth
Photosynthesis
plant growth
Chloroplasts
RNA Interference
leaves
chloroplasts
photosynthesis
Agrobacterium
Holoenzymes
Protein Subunits
protein subunits
Arabidopsis
Zea mays
ultrastructure

Keywords

  • RuBP carboxylation
  • chaperone
  • photosynthesis
  • protein folding

ASJC Scopus subject areas

  • Physiology
  • Plant Science

Cite this

BSD2 is a Rubisco-specific assembly chaperone, forms intermediary hetero-oligomeric complexes, and is nonlimiting to growth in tobacco. / Conlan, Brendon; Birch, Rosemary; Kelso, Celine; Holland, Sophie; De Souza, Amanda P.; Long, Stephen P; Beck, Jennifer L.; Whitney, Spencer M.

In: Plant Cell and Environment, Vol. 42, No. 4, 04.2019, p. 1287-1301.

Research output: Contribution to journalArticle

Conlan, Brendon ; Birch, Rosemary ; Kelso, Celine ; Holland, Sophie ; De Souza, Amanda P. ; Long, Stephen P ; Beck, Jennifer L. ; Whitney, Spencer M. / BSD2 is a Rubisco-specific assembly chaperone, forms intermediary hetero-oligomeric complexes, and is nonlimiting to growth in tobacco. In: Plant Cell and Environment. 2019 ; Vol. 42, No. 4. pp. 1287-1301.
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