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  Mechanism of Enzyme Repair by the AAA(+) Chaperone Rubisco Activase

Bhat, J. Y., Milicic, G., Thieulin-Pardo, G., Bracher, A., Maxwell, A., Ciniawsky, S., et al. (2017). Mechanism of Enzyme Repair by the AAA(+) Chaperone Rubisco Activase. Molecular Cell, 67(5), 744-756.e6. doi:10.1016/j.molcel.2017.07.004.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-77B4-F Version Permalink: http://hdl.handle.net/21.11116/0000-0000-77B5-E
Genre: Journal Article

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 Creators:
Bhat, Javaid Y.1, Author              
Milicic, Goran1, Author              
Thieulin-Pardo, Gabriel1, Author              
Bracher, Andreas1, Author              
Maxwell, Andrew1, Author              
Ciniawsky, Susanne2, Author
Mueller-Cajar, Oliver1, Author              
Engen, John R.2, Author
Hartl, F. Ulrich1, Author              
Wendler, Petra2, Author
Hayer-Hartl, Manajit3, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2external, ou_persistent22              
3Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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Free keywords: EXCHANGE-MASS-SPECTROMETRY; RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE; HYDROGEN-EXCHANGE; ELECTRON-MICROSCOPY; STRUCTURE ELUCIDATION; INTERACTION NETWORKS; CROSS-LINKING; VISUALIZATION; INTERMEDIATE; BISPHOSPHATEBiochemistry & Molecular Biology; Cell Biology;
 Abstract: How AAA(+) chaperones conformationally remodel specific target proteins in an ATP-dependent manner is not well understood. Here, we investigated the mechanism of the AAA(+) protein Rubisco activase (Rca) in metabolic repair of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits containing eight catalytic sites. Rubisco is prone to inhibition by tight-binding sugar phosphates, whose removal is catalyzed by Rca. We engineered a stable Rca hexamer ring and analyzed its functional interaction with Rubisco. Hydrogen/deuterium exchange and chemical crosslinking showed that Rca structurally destabilizes elements of the Rubisco active site with remarkable selectivity. Cryo-electron microscopy revealed that Rca docks onto Rubisco over one active site at a time, positioning the C-terminal strand of RbcL, which stabilizes the catalytic center, for access to the Rca hexamer pore. The pulling force of Rca is fine-tuned to avoid global destabilization and allow for precise enzyme repair.

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Language(s): eng - English
 Dates: 2017-08-102017-09
 Publication Status: Published in print
 Pages: 19
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Degree: -

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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 67 (5) Sequence Number: - Start / End Page: 744 - 756.e6 Identifier: ISSN: 1097-2765
CoNE: /journals/resource/954925610929