The proteasome antechamber maintains substrates in an unfolded state

Amy M. Ruschak, Tomasz L. Religa, Sarah Breuer, Susanne Witt and Lewis E. Kay ()
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Amy M. Ruschak: Biochemistry and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada
Tomasz L. Religa: Biochemistry and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada
Sarah Breuer: Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
Susanne Witt: Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
Lewis E. Kay: Biochemistry and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada

Nature, 2010, vol. 467, issue 7317, 868-871

Abstract: Proteasome antechamber hosts unfolded proteins The proteasome is a multi-protein complex that degrades proteins enzymatically. Proteolysis occurs in a barrel-shaped 20S core particle comprising three interconnected cavities, including a pair of antechambers in which substrates are held before degradation. In this study, Lewis Kay and colleagues demonstrate that substrates interact actively with the antechamber walls, and that the environment in this compartment is optimized to maintain the substrate in an unfolded 'ready to eat' state, easily accessible for hydrolysis.

Date: 2010
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DOI: 10.1038/nature09444

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