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  Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii

Bracher, A., Hauser, T., Liu, C., Hartl, F. U., & Hayer-Hartl, M. (2015). Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii. PLOS ONE, 10(8): e0135448. doi:10.1371/journal.pone.0135448.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-514F-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-5150-2
Genre: Journal Article

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 Creators:
Bracher, Andreas1, Author              
Hauser, Thomas2, Author              
Liu, Cuimin1, Author              
Hartl, F. Ulrich1, Author              
Hayer-Hartl, Manajit2, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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Free keywords: ESCHERICHIA-COLI; RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE; THERMOSYNECHOCOCCUS-ELONGATUS; HEXADECAMERIC RUBISCO; ARABIDOPSIS-THALIANA; FORM-I; PROTEIN; BIOGENESIS; TOOLS; PLANT
 Abstract: The most prevalent form of the Rubisco enzyme is a complex of eight catalytic large sub-units (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 RbcL(8) 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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Language(s): eng - English
 Dates: 2015
 Publication Status: Published online
 Pages: 17
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 Rev. Type: Peer
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Title: PLOS ONE
Source Genre: Journal
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Publ. Info: 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA : PUBLIC LIBRARY SCIENCE
Pages: - Volume / Issue: 10 (8) Sequence Number: e0135448 Start / End Page: - Identifier: ISSN: 1932-6203