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Article

In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome.

The EMBO journal - 15 Aug 1997

Amerik AYu, Swaminathan S, Krantz B A, Wilkinson K D, Hochstrasser M

Abstract excerpt

Degradation of many eukaryotic proteins requires their prior ligation to polyubiquitin chains, which target substrates to the 26S proteasome, an abundant cellular protease. We describe a yeast deubiquitinating enzyme, Ubp14, that specifically disassembles unanchored ('free') ubiquitin chains in vitro, a specificity shared by mammalian isopeptidase T. Correspondingly, deletion of the UBP14 gene from yeast cells...

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Identifiers

PMID: 9305625
DOI: 10.1093/emboj/16.16.4826
PMCID: PMC1170118

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