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Updated: Oct 22, 2025

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
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Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

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プロテアソーム組立中の障害をモニターする品質管理因子の特定

Eszter Zavodszky1, Sew-Yeu Peak-Chew1, Szymon Juszkiewicz1

  • 1MRC Laboratory of Molecular Biology, Cambridge, UK.

Science (New York, N.Y.)
|August 27, 2021
PubMed
まとめ

PSMC5のような過剰なプロテアソームサブユニットは,PAAF1チャペロンによって特定されたHERC1ユビキチンリガゼによって分解されます. このメカニズムは,組立していない中間物質を除去することによって,タンパク質の恒常性を維持します.

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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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