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Studying Protein Ubiquitylation in Yeast
- Source :
- Methods in Molecular Biology ISBN: 9781493937547, Proteostasis: Methods and Protocols, Proteostasis: Methods and Protocols, pp.117-142, 2016, ⟨10.1007/978-1-4939-3756-1_5⟩
- Publication Year :
- 2016
- Publisher :
- Springer New York, 2016.
-
Abstract
- Ubiquitylation is a reversible posttranslational modification that is critical for most, if not all, cellular processes and essential for viability. Ubiquitin conjugates to substrate proteins either as a single moiety (monoubiquitylation) or as polymers composed of ubiquitin molecules linked to each other with various topologies and structures (polyubiquitylation). This contributes to an elaborate ubiquitin code that is decrypted by specific ubiquitin-binding proteins. Indeed, these different types of ubiquitylation have different functional outcomes, notably affecting the stability of the substrate, its interactions, its activity, or its subcellular localization. In this chapter, we describe protocols to determine whether a protein is ubiquitylated, to identify the site that is ubiquitylated, and provide direction to study the topology of the ubiquitin modification, in the yeast Saccharomyces cerevisiae.
- Subjects :
- 0301 basic medicine
biology
Chemistry
Saccharomyces cerevisiae
Substrate (chemistry)
[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]
Subcellular localization
biology.organism_classification
Yeast
Cell biology
03 medical and health sciences
030104 developmental biology
Protein ubiquitylation
Ubiquitin
Posttranslational modification
biology.protein
Moiety
ComputingMilieux_MISCELLANEOUS
Subjects
Details
- ISBN :
- 978-1-4939-3754-7
- ISBNs :
- 9781493937547
- Database :
- OpenAIRE
- Journal :
- Methods in Molecular Biology ISBN: 9781493937547, Proteostasis: Methods and Protocols, Proteostasis: Methods and Protocols, pp.117-142, 2016, ⟨10.1007/978-1-4939-3756-1_5⟩
- Accession number :
- edsair.doi.dedup.....4b35fe6164e4903d9807931e44a667cf