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Tytuł:
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BSD2 is a Rubisco-specific assembly chaperone, forms intermediary hetero-oligomeric complexes, and is nonlimiting to growth in tobacco.
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Autorzy:
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Conlan B; Research School of Biology, The Australian National University, Acton, Australian Capital Territory, Australia.
Birch R; Research School of Biology, The Australian National University, Acton, Australian Capital Territory, Australia.
Kelso C; School of Chemistry, Molecular Horizons, University of Wollongong, New South Wales, Australia.
Holland S; Research School of Biology, The Australian National University, Acton, Australian Capital Territory, Australia.
De Souza AP; Carl R. Woese Institute for Genomic Biology, University of Illinois, Urbana, Illinois, USA.
Long SP; Carl R. Woese Institute for Genomic Biology, University of Illinois, Urbana, Illinois, USA.; Lancaster Environment Centre, Lancaster University, Lancaster, UK.
Beck JL; School of Chemistry, Molecular Horizons, University of Wollongong, New South Wales, Australia.
Whitney SM; Research School of Biology, The Australian National University, Acton, Australian Capital Territory, Australia.
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Źródło:
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Plant, cell & environment [Plant Cell Environ] 2019 Apr; Vol. 42 (4), pp. 1287-1301. Date of Electronic Publication: 2018 Nov 20.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Publication: Hoboken, NJ : John Wiley & Sons Ltd.
Original Publication: Oxford, UK : Blackwell Scientific Publications
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MeSH Terms:
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Molecular Chaperones/*metabolism
Plant Proteins/*metabolism
Ribulose-Bisphosphate Carboxylase/*metabolism
Nicotiana/*metabolism
Molecular Chaperones/physiology ; Plant Leaves/metabolism ; Plant Proteins/physiology ; Plants, Genetically Modified ; Nicotiana/growth & development
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Grant Information:
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OPP1060461 United States GATES Bill & Melinda Gates Foundation
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Contributed Indexing:
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Keywords: RuBP carboxylation; chaperone; photosynthesis; protein folding
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Substance Nomenclature:
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0 (Molecular Chaperones)
0 (Plant Proteins)
EC 4.1.1.39 (Ribulose-Bisphosphate Carboxylase)
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Entry Date(s):
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Date Created: 20181031 Date Completed: 20200323 Latest Revision: 20231213
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Update Code:
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20240105
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DOI:
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10.1111/pce.13473
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PMID:
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30375663
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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.
(© 2018 John Wiley & Sons Ltd.)
