Journal
PLANT JOURNAL
Volume 98, Issue 5, Pages 798-812Publisher
WILEY
DOI: 10.1111/tpj.14273
Keywords
chaperonin; rubisco; protein folding; photosynthesis; CPN60
Categories
Funding
- National Natural Science Foundation of China [31671262, 31670754]
- National Basic Research Program of China (973 Program) [2015CB150106-1, 2017YFA0503503]
- Deutsche Forschungsgemeinschaft [TRR175]
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The chloroplast chaperonin system is indispensable for the biogenesis of Rubisco, the key enzyme in photosynthesis. Using Chlamydomonas reinhardtii as a model system, we found that in vivo the chloroplast chaperonin consists of CPN60 alpha, CPN60 beta 1 and CPN60 beta 2 and the co-chaperonin of the three subunits CPN20, CPN11 and CPN23. In Escherichia coli, CPN20 homo-oligomers and all possible other chloroplast co-chaperonin hetero-oligomers are functional, but only that consisting of CPN11/20/23-CPN60 alpha beta 1 beta 2 can fully replace GroES/GroEL under stringent stress conditions. Endogenous CPN60 was purified and its stoichiometry was determined to be 6:2:6 for CPN60 alpha:CPN60 beta 1:CPN60 beta 2. The cryo-EM structures of endogenous CPN60 alpha beta 1 beta 2/ADP and CPN60 alpha beta 1 beta 2/co-chaperonin/ADP were solved at resolutions of 4.06 and 3.82 angstrom, respectively. In both hetero-oligomeric complexes the chaperonin subunits within each ring are highly symmetric. Through hetero-oligomerization, the chloroplast co-chaperonin CPN11/20/23 forms seven GroES-like domains, which symmetrically interact with CPN60 alpha beta 1 beta 2. Our structure also reveals an uneven distribution of roof-forming domains in the dome-shaped CPN11/20/23 co-chaperonin and potentially diversified surface properties in the folding cavity of the CPN60 alpha beta 1 beta 2 chaperonin that might enable the chloroplast chaperonin system to assist in the folding of specific substrates.
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