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

Wietrzynski, W., Traverso, E., Wollman, F.-A., & Wostrikoff, K. (2021). The state of oligomerization of Rubisco controls the rate of synthesis of the Rubisco large subunit in Chlamydomonas reinhardtii. Plant Cell, 33(5), 1706-1727. doi:10.1093/plcell/koab061.

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 Creators:
Wietrzynski, Wojciech1, Author           
Traverso, Eleonora2, Author
Wollman, Francis-Andre2, Author
Wostrikoff, Katia2, Author
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

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Free keywords: RIBULOSE-BISPHOSPHATE CARBOXYLASE; BUNDLE-SHEATH DEFECTIVE2; RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE; MESSENGER-RNA; ASSEMBLY CHAPERONE; CRYSTAL-STRUCTURE; OXIDATIVE STRESS; GENE-EXPRESSION; MESOPHYLL-CELLS; CYTOCHROME FBiochemistry & Molecular Biology; Plant Sciences; Cell Biology;
 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.

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Language(s): eng - English
 Dates: 2021
 Publication Status: Published in print
 Pages: 22
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000674746200024
DOI: 10.1093/plcell/koab061
 Degree: -

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Title: Plant Cell
  Abbreviation : Plant C
Source Genre: Journal
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Publ. Info: Rockville : American Society of Plant Physiologists
Pages: - Volume / Issue: 33 (5) Sequence Number: - Start / End Page: 1706 - 1727 Identifier: ISSN: 1532-298X
CoNE: https://pure.mpg.de/cone/journals/resource/1532-298X