Molecular basis for the assembly of RuBisCO assisted by the chaperone Raf1
| Autor: | Wen-Wen Kong, Hui Sun, Wei-Fang Li, Ling-Yun Xia, Yuxing Chen, Yong-Liang Jiang, Cong-Zhao Zhou |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
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 |
| Zdroj: | Nature Plants. 6:708-717 |
| ISSN: | 2055-0278 |
| DOI: | 10.1038/s41477-020-0665-8 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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