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

Bhat, Javaid Y.; Milicic, Goran; Thieulin-Pardo, Gabriel; Bracher, Andreas; Maxwell, Andrew; Ciniawsky, Susanne; Mueller-Cajar, Oliver; Engen, John R.; Hartl, F. Ulrich; Wendler, Petra; Hayer-Hartl, Manajit

doi:10.1016/j.molcel.2017.07.004

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

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Bhat, Javaid Y.
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Milicic, Goran
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Thieulin-Pardo, Gabriel
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77798

Bracher, Andreas
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Maxwell, Andrew
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Mueller-Cajar, Oliver
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Hartl, F. Ulrich
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Hayer-Hartl, Manajit
Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

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.

Cite as: https://hdl.handle.net/21.11116/0000-0000-77B4-F

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.