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Publication . Article . Other literature type . 2021

The state of oligomerization of Rubisco controls the rate of synthesis of the Rubisco large subunit in Chlamydomonas reinhardtii

Wojciech Wietrzynski; Eleonora Traverso; Francis-André Wollman; Katia Wostrikoff;
Open Access
Published: 24 Feb 2021
Publisher: Oxford University Press
ABSTRACT Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) is present in all photosynthetic organisms and is a key enzyme for photosynthesis-driven life on Earth. Its most prominent form is a hetero-oligomer in which small subunits (SSU) stabilize the core of the enzyme built from large subunits (LSU), yielding, after a chaperone-assisted multistep assembly process, an LSU8SSU8 hexadecameric holoenzyme. Here we use Chlamydomonas reinhardtii and a combination of site-directed mutants to dissect the multistep biogenesis pathway of Rubisco in vivo. We identify assembly intermediates, in two of which LSU are associated with the RAF1 chaperone. Using genetic and biochemical approaches we further unravel a major regulation process during Rubisco biogenesis, in which LSU translation is controlled by its ability to assemble with the SSU, via the mechanism of control by epistasy of synthesis (CES). Altogether this leads us to propose a model whereby the last assembly intermediate, an LSU8-RAF1 complex, provides the platform for SSU binding to form the Rubisco enzyme, and when SSU is not available, converts to a key regulatory form that exerts negative feedback on the initiation of LSU translation.
Subjects by Vocabulary

Medical Subject Headings: fungi parasitic diseases

Microsoft Academic Graph classification: RuBisCO biology.protein biology Mutant Ribulose chemistry.chemical_compound chemistry Chaperone (protein) Chlamydomonas reinhardtii biology.organism_classification Protein subunit Biogenesis Biochemistry Translation (biology)


Research Articles, Cell Biology, Plant Science, [SDV]Life Sciences [q-bio]