Proteome Turnover Analysis in Haloferax volcanii by a Heavy Isotope Multilabeling Approach.
Haloarchaea
Haloferax volcanii
Mass spectrometry
Metabolic labeling
Proteome turnover
Proteomics
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2022
2022
Historique:
entrez:
20
9
2022
pubmed:
21
9
2022
medline:
24
9
2022
Statut:
ppublish
Résumé
The cellular protein repertoire is highly dynamic and responsive to internal or external stimuli. Its changes are largely the consequence of the combination of protein synthesis and degradation, referred collectively as protein turnover. Different proteomics techniques have been developed to determine the whole proteome turnover of a cell, but very few have been applied to archaea. In this chapter we describe a heavy isotope multilabeling method that allowed the successful analysis of relative protein synthesis and degradation rates on the proteome scale of the halophilic archaeon Haloferax volcanii. This method combines
Identifiants
pubmed: 36125756
doi: 10.1007/978-1-0716-2445-6_17
doi:
Substances chimiques
Isotopes
0
Proteome
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
267-286Informations de copyright
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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