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  Structure and mechanism of the Rubisco-assembly chaperone Raf1

Hauser, T., Bhat, J. Y., Milicic, G., Wendler, P., Hartl, F. U., Bracher, A., et al. (2015). Structure and mechanism of the Rubisco-assembly chaperone Raf1. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 22(9), 720-728. doi:10.1038/nsmb.3062.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-953F-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-9540-9
Genre: Journal Article

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 Creators:
Hauser, Thomas1, Author              
Bhat, Javaid Y.2, Author              
Milicic, Goran2, Author              
Wendler, Petra3, Author
Hartl, F. Ulrich2, Author              
Bracher, Andreas2, Author              
Hayer-Hartl, Manajit1, Author              
Affiliations:
1Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              
2Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
3external, ou_persistent22              

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Free keywords: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE; ESCHERICHIA-COLI; RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE; HEXADECAMERIC RUBISCO; CLUSTAL-W; RBCX GENE; PROTEIN; PHOTOSYNTHESIS; SCATTERING; SYSTEM
 Abstract: Biogenesis of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits, requires assembly chaperones. Here we analyzed the role of Rubisco accumulation factor1 (Raf1), a dimer of similar to 40-kDa subunits. We find that Raf1 from Synechococcus elongatus acts downstream of chaperonin-assisted RbcL folding by stabilizing RbcL antiparallel dimers for assembly into RbcL(8) complexes with four Raf1 dimers bound. Raf1 displacement by RbcS results in holoenzyme formation. Crystal structures show that Raf1 from Arabidopsis thaliana consists of a beta-sheet dimerization domain and a flexibly linked alpha-helical domain. Chemical cross-linking and EM reconstruction indicate that the beta-domains bind along the equator of each RbcL(2) unit, and the alpha-helical domains embrace the top and bottom edges of RbcL(2). Raf1 fulfills a role similar to that of the assembly chaperone RbcX, thus suggesting that functionally redundant factors ensure efficient Rubisco biogenesis.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000360933200015
DOI: 10.1038/nsmb.3062
 Degree: -

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Title: NATURE STRUCTURAL & MOLECULAR BIOLOGY
Source Genre: Journal
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Publ. Info: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 22 (9) Sequence Number: - Start / End Page: 720 - 728 Identifier: ISSN: 1545-9993