A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein

Vincent Chau, John W. Tobias, Andreas Bachmair, David Marriott, David J. Ecker, David K. Gonda, Alexander Varshavsky

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Abstract

The ubiquitin-dependent degradation of a test protein β-galactosidase (βgal) is preceded by ubiquitination of βgal. The many (from 1 to more than 20) ubiquitin moieties attached to a molecule of βgal occur as an ordered chain of branched ubiquitin-ubiquitin conjugates in which the carboxyl-terminal Gly76 of one ubiquitin is joined to the internal Lys48 of an adjacent ubiquitin. This multiubiquitin chain is linked to one of two specific Lys residues in βgal. These same Lys residues have been identified by molecular genetic analysis as components of the amino-terminal degradation signal in βgal. The experiments with ubiquitin mutated at its Lys48 residue indicate that the multiubiquitin chain in a targeted protein is essential for the degradation of the protein.

Original languageEnglish (US)
Pages (from-to)1576-1583
Number of pages8
JournalScience
Volume243
Issue number4898
DOIs
StatePublished - Jan 1 1989

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All Science Journal Classification (ASJC) codes

  • General

Cite this

Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989). A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science, 243(4898), 1576-1583. https://doi.org/10.1126/science.2538923