ArticlePloS one2015
Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Targeted genetic manipulation and yeast-like evolutionary genomics in the green alga Auxenochlorella.The Plant cell · 2025Article
- Targeted genetic manipulation and yeast-like evolutionary genomics in the green algabioRxiv : the preprint server for biology · 2025Article
- Strategies to improve photosynthesis by modifying the RuBisCO system and its limitations.Molecular biology reports · 2025Review
- Transit Peptides Often Require Downstream Unstructured Sequence for Efficient Chloroplast Import inFrontiers in plant science · 2022Article
- The state of oligomerization of Rubisco controls the rate of synthesis of the Rubisco large subunit in Chlamydomonas reinhardtii.The Plant cell · 2021Article
- Article
- Exceptionally high rates of positive selection on the rbcL gene in the genus Ilex (Aquifoliaceae).BMC evolutionary biology · 2019Article
- Roles of RbcX in Carboxysome Biosynthesis in the CyanobacteriumPlant physiology · 2019Article
- Rubisco Assembly in the Chloroplast.Frontiers in molecular biosciences · 2018Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The most prevalent form of the Rubisco enzyme is a complex of eight catalytic large subunits (RbcL) and eight regulatory small subunits (RbcS). Rubisco biogenesis depends on the assistance by specific molecular chaperones. The assembly chaperone RbcX stabilizes the RbcL subunits after folding by chaperonin and mediates their assembly to the RbcL8 core complex, from which RbcX is displaced by RbcS to form active holoenzyme. Two isoforms of RbcX are found in eukaryotes, RbcX-I, which is more closely related to cyanobacterial RbcX, and the more distant RbcX-II. The green algae Chlamydomonas reinhardtii contains only RbcX-II isoforms, CrRbcX-IIa and CrRbcX-IIb. Here we solved the crystal structure of CrRbcX-IIa and show that it forms an arc-shaped dimer with a central hydrophobic cleft for binding the C-terminal sequence of RbcL. Like other RbcX proteins, CrRbcX-IIa supports the assembly of cyanobacterial Rubisco in vitro, albeit with reduced activity relative to cyanobacterial RbcX-I. Structural analysis of a fusion protein of CrRbcX-IIa and the C-terminal peptide of RbcL suggests that the peptide binding mode of RbcX-II may differ from that of cyanobacterial RbcX. RbcX homologs appear to have adapted to their cognate Rubisco clients as a result of co-evolution.
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