| Range |
Table - link
|
| Organism |
Yeast |
| Reference |
Christiano R, Nagaraj N, Fröhlich F, Walther TC. Global proteome turnover analyses of the Yeasts S. cerevisiae and S. pombe. Cell Rep. 2014 Dec 11 9(5):1959-65. doi: 10.1016/j.celrep.2014.10.065. Supplemental Information p.S11 table S3PubMed ID25466257
|
| Primary Source |
See refs beneath table |
| Method |
p.1959 right column bottom paragraph:"To determine protein turnover rates systematically, [investigators] metabolically labeled the yeasts with heavy isotopes containing lysine (“heavy” lysine, H) and diluted the cells in an excess of normal lysine (“light” lysine, L) at the beginning of the experiment (Figures 1A, S1A, and S1B). [They] analyzed the decay of the heavy lysine signal in the proteome over time by high-resolution mass spectrometry-based proteomics (Schwanhäusser et al., 2011) (Figure 1B)." |
| Comments |
P.1960 left column bottom paragraph to right column top paragraph:"As observed in other model systems (Doherty et al., 2009), the distribution of half-lives in both species does not follow a normal distribution but is skewed with more short-lived proteins (Kolmogorov-Smirnov test, p < 2.2 × 10^−16). [Investigators’] results were further validated by comparing [their] data set to known turnover rates determined by other experimental approaches, such as pulse chase with radioactively labeled amino acids (Table S3). In addition, comparative analysis of each protein’s turnover rate also highlighted problems with measuring the half-lives of tagged proteins during cycloheximide treatment with significant deviations from the rates measured by [their] proteomics approach. This might be due to altered cell physiology during protein synthesis inhibition and/or the modification of proteins with tags (Belle et al., 2006) (Figures S2A and S2B)." |
| Entered by |
Uri M |
| ID |
112047 |