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TitleRubisco accumulation factor 1 (Raf1) plays essential roles in mediating Rubisco assembly and carboxysome biogenesis.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 117, Issue 29, Page 17418-17428, Year 2020
Publish dateJul 21, 2020
AuthorsFang Huang / Wen-Wen Kong / Yaqi Sun / Taiyu Chen / Gregory F Dykes / Yong-Liang Jiang / Lu-Ning Liu /
PubMed AbstractCarboxysomes are membrane-free organelles for carbon assimilation in cyanobacteria. The carboxysome consists of a proteinaceous shell that structurally resembles virus capsids and internal enzymes ...Carboxysomes are membrane-free organelles for carbon assimilation in cyanobacteria. The carboxysome consists of a proteinaceous shell that structurally resembles virus capsids and internal enzymes including ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco), the primary carbon-fixing enzyme in photosynthesis. The formation of carboxysomes requires hierarchical self-assembly of thousands of protein subunits, initiated from Rubisco assembly and packaging to shell encapsulation. Here we study the role of Rubisco assembly factor 1 (Raf1) in Rubisco assembly and carboxysome formation in a model cyanobacterium, PCC7942 (Syn7942). Cryo-electron microscopy reveals that Raf1 facilitates Rubisco assembly by mediating RbcL dimer formation and dimer-dimer interactions. Syn7942 cells lacking Raf1 are unable to form canonical intact carboxysomes but generate a large number of intermediate assemblies comprising Rubisco, CcaA, CcmM, and CcmN without shell encapsulation and a low abundance of carboxysome-like structures with reduced dimensions and irregular shell shapes and internal organization. As a consequence, the Raf1-depleted cells exhibit reduced Rubisco content, CO-fixing activity, and cell growth. Our results provide mechanistic insight into the chaperone-assisted Rubisco assembly and biogenesis of carboxysomes. Advanced understanding of the biogenesis and stepwise formation process of the biogeochemically important organelle may inform strategies for heterologous engineering of functional CO-fixing modules to improve photosynthesis.
External linksProc Natl Acad Sci U S A / PubMed:32636267 / PubMed Central
MethodsEM (single particle)
Resolution4.3 Å
Structure data

10235

6smh

EMDB-10235, PDB-6smh:
Cryo-electron microscopy structure of a RbcL-Raf1 supercomplex from Synechococcus elongatus PCC 7942
Method: EM (single particle) / Resolution: 4.3 Å

Source
  • Synechococcus elongatus PCC 7942 (bacteria)
  • Synechococcus elongatus PCC 7942 = FACHB-805 (bacteria)
  • synechococcus elongatus (strain pcc 7942 / fachb-805) (bacteria)
KeywordsPHOTOSYNTHESIS / Rubisco / Rubisco accumulation factor1 / Raf1 / Synechococcus elongatus 7942 / Cyanobacteria

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