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New crystal structure of the proteasome‐dedicated chaperone Rpn14 at 1.6 Å resolution

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Abstract:

The 26S proteasome is an ATP‐dependent protease responsible for selective degradation of polyubiquitylated proteins. Recent studies have suggested that proteasome assembly is a highly ordered multi‐step process assisted by specific chaperones. Rpn14, an assembly chaperone for ATPase‐ring formation, specifically recognizes the ATPase subunit Rpt6. The structure of Rpn14 at 2.0 Å resolution in space group P64 has previously been reported, but the detailed mechanism of Rpn14 function remains unclear. Here, a new crystal structure of Rpn14 with an E384A mutation is presented in space group P21 at 1.6 Å resolution. This high‐resolution structure provides a framework for understanding proteasome assembly.

Document Type: Research Article

DOI: https://doi.org/10.1107/S1744309112011359

Publication date: 2012-05-01

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