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Molecular basis for the assembly of RuBisCO assisted by the chaperone Raf1
- Source :
- Nature Plants. 6:708-717
- Publication Year :
- 2020
- Publisher :
- Springer Science and Business Media LLC, 2020.
-
Abstract
- The folding and assembly of RuBisCO, the most abundant enzyme in nature, needs a series of chaperones, including the RuBisCO accumulation factor Raf1, which is highly conserved in cyanobacteria and plants. Here, we report the crystal structures of Raf1 from cyanobacteria Anabaena sp. PCC 7120 and its complex with RuBisCO large subunit RbcL. Structural analyses and biochemical assays reveal that each Raf1 dimer captures an RbcL dimer, with the C-terminal tail inserting into the catalytic pocket, and further mediates the assembly of RbcL dimers to form the octameric core of RuBisCO. Furthermore, the cryo-electron microscopy structures of the RbcL-Raf1-RbcS assembly intermediates enable us to see a dynamic assembly process from RbcL8Raf18 to the holoenzyme RbcL8RbcS8. In vitro assays also indicate that Raf1 can attenuate and reverse CcmM-mediated cyanobacterial RuBisCO condensation. Combined with previous findings, we propose a putative model for the assembly of cyanobacterial RuBisCO coordinated by the chaperone Raf1.
- Subjects :
- inorganic chemicals
0106 biological sciences
0301 basic medicine
Cyanobacteria
biology
Chemistry
Protein subunit
Dimer
fungi
RuBisCO
food and beverages
Sequence alignment
Plant Science
biology.organism_classification
01 natural sciences
03 medical and health sciences
chemistry.chemical_compound
030104 developmental biology
Protein structure
Chaperone (protein)
biology.protein
Biophysics
Peptide sequence
010606 plant biology & botany
Subjects
Details
- ISSN :
- 20550278
- Volume :
- 6
- Database :
- OpenAIRE
- Journal :
- Nature Plants
- Accession number :
- edsair.doi...........cc0b96f11e173b52124032c59641162b