Proteome Turnover Analysis in Haloferax volcanii by a Heavy Isotope Multilabeling Approach.
Methods Mol Biol
; 2522: 267-286, 2022.
Article
em En
| MEDLINE
| ID: mdl-36125756
ABSTRACT
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 15N and 13C isotope metabolic labeling with high-resolution mass spectrometry and data analysis tools (QuPE web-based platform) and could be applied to different archaea.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Haloferax volcanii
Idioma:
En
Revista:
Methods Mol Biol
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2022
Tipo de documento:
Article
País de afiliação:
Argentina