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.
Paggi, R.A., Albaum, S.P., Poetsch, A., Cerletti, M. (2022). Proteome Turnover Analysis in Haloferax volcanii by a Heavy Isotope Multilabeling Approach. In: Ferreira-Cerca, S. (eds) Archaea. Methods in Molecular Biology, vol 2522. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2445-6_17
Link to chapter:https://link.springer.com/protocol/10.1007/978-1-0716-2445-6_17