Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85
- PMID: 6327059
- DOI: 10.1016/0092-8674(84)90299-x
Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85
Abstract
Ubiquitin, a 76 residue protein, occurs in eucaryotic cells either free or covalently joined to a variety of protein species. Previous work suggested that ubiquitin may function as a signal for attack by proteinases specific for ubiquitin-protein conjugates. We show that the mouse cell line ts85 , a previously isolated cell cycle mutant, is temperature-sensitive in ubiquitin-protein conjugation, and that this effect is due to the specific thermolability of the ts85 ubiquitin-activating enzyme (E1). From E1 thermoinactivation kinetics in mixed (wild-type plus ts85 ) extracts, and from copurification of the determinant of E1 thermolability with E1 in ubiquitin-affinity chromatography, we conclude that the determinant of E1 thermolability is contained within the E1 polypeptide. ts85 cells fail to degrade otherwise short-lived intracellular proteins at the nonpermissive temperature (accompanying paper), demonstrating that degradation of the bulk of short-lived proteins in this higher eucaryotic cell proceeds through a ubiquitin-dependent pathway. We discuss possible roles of ubiquitin-dependent pathways in DNA transactions, the cell cycle, and the heat shock response.
Comment in
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Back to the future with ubiquitin.Cell. 2004 Jan 23;116(2):181-90. doi: 10.1016/s0092-8674(03)01074-2. Cell. 2004. PMID: 14744430 Review.
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Ubiquitin as a central cellular regulator.Cell. 2004 Jan 23;116(2 Suppl):S29-32, 2 p following S32. doi: 10.1016/s0092-8674(03)00971-1. Cell. 2004. PMID: 15055578 No abstract available.
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