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Sch9 regulates intracellular protein ubiquitination by controlling stress responses.

Qie B, Lyu Z, Lyu L, Liu J, Gao X, Liu Y, Duan W, Zhang N, Du L, Liu K - Redox Biol (2015)

Bottom Line: In this study, we found that the overall level of ubiquitinated proteins dramatically decreased as yeast cell grew from log to stationary phase.Deletion of SCH9, a gene encoding a key protein kinase for longevity control, decreased the level of ubiquitinated proteins in log phase and this effect could be reversed by restoring Sch9 function.Our results revealed for the first time how Sch9 regulates the level of ubiquitinated proteins and provides new insight into how Sch9 controls longevity.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Bio-Resources and Eco-Environment of Ministry of Education, College of Life Science, Sichuan University, Chengdu, Sichuan 610064, China.

No MeSH data available.


Related in: MedlinePlus

Decreased protein carbonylation by alleviated intracellular oxidation in sch9Δ cells. (A) Measurements of concentration of protein carbonyl groups in WT cells (TB50a) transformed with empty vector (WT + vector), SCH9 deletion mutant cells (TS120-2d) transformed with empty vector (sch9Δ+vector) or pRS416−SCH9 (sch9Δ+Sch9) in log or stationary phase. (B) Fluorescence spectrometer analysis of DCF-stained WT (TB50a) and sch9Δ cells in log or stationary phase. (C) Microscopy of DCF-stained WT (TB50a) and sch9Δ cells in log or stationary phase. Bars: 100 µm (log phase cells were collected 12–16 h after inoculation with an OD600nm of 0.5 while stationary phase cells were collected 72 h after inoculation with an OD600 nm of 8–9. *p < 0.05, **p < 0.01).
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f0030: Decreased protein carbonylation by alleviated intracellular oxidation in sch9Δ cells. (A) Measurements of concentration of protein carbonyl groups in WT cells (TB50a) transformed with empty vector (WT + vector), SCH9 deletion mutant cells (TS120-2d) transformed with empty vector (sch9Δ+vector) or pRS416−SCH9 (sch9Δ+Sch9) in log or stationary phase. (B) Fluorescence spectrometer analysis of DCF-stained WT (TB50a) and sch9Δ cells in log or stationary phase. (C) Microscopy of DCF-stained WT (TB50a) and sch9Δ cells in log or stationary phase. Bars: 100 µm (log phase cells were collected 12–16 h after inoculation with an OD600nm of 0.5 while stationary phase cells were collected 72 h after inoculation with an OD600 nm of 8–9. *p < 0.05, **p < 0.01).

Mentions: To investigate the correlation between decreased oxidative stress and protein ubiquitination in sch9Δ cells, the concentrations of carbonyl groups in oxidized intracellular proteins in WT and sch9Δ cells were evaluated. In log phase, the level of protein carbonyl in sch9Δ cells was ~30% lower than that in WT cells. Adding Sch9 back restored the level of protein carbonyl to a similar level as that in wild type cells (Fig. 6A).


Sch9 regulates intracellular protein ubiquitination by controlling stress responses.

Qie B, Lyu Z, Lyu L, Liu J, Gao X, Liu Y, Duan W, Zhang N, Du L, Liu K - Redox Biol (2015)

Decreased protein carbonylation by alleviated intracellular oxidation in sch9Δ cells. (A) Measurements of concentration of protein carbonyl groups in WT cells (TB50a) transformed with empty vector (WT + vector), SCH9 deletion mutant cells (TS120-2d) transformed with empty vector (sch9Δ+vector) or pRS416−SCH9 (sch9Δ+Sch9) in log or stationary phase. (B) Fluorescence spectrometer analysis of DCF-stained WT (TB50a) and sch9Δ cells in log or stationary phase. (C) Microscopy of DCF-stained WT (TB50a) and sch9Δ cells in log or stationary phase. Bars: 100 µm (log phase cells were collected 12–16 h after inoculation with an OD600nm of 0.5 while stationary phase cells were collected 72 h after inoculation with an OD600 nm of 8–9. *p < 0.05, **p < 0.01).
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4477112&req=5

f0030: Decreased protein carbonylation by alleviated intracellular oxidation in sch9Δ cells. (A) Measurements of concentration of protein carbonyl groups in WT cells (TB50a) transformed with empty vector (WT + vector), SCH9 deletion mutant cells (TS120-2d) transformed with empty vector (sch9Δ+vector) or pRS416−SCH9 (sch9Δ+Sch9) in log or stationary phase. (B) Fluorescence spectrometer analysis of DCF-stained WT (TB50a) and sch9Δ cells in log or stationary phase. (C) Microscopy of DCF-stained WT (TB50a) and sch9Δ cells in log or stationary phase. Bars: 100 µm (log phase cells were collected 12–16 h after inoculation with an OD600nm of 0.5 while stationary phase cells were collected 72 h after inoculation with an OD600 nm of 8–9. *p < 0.05, **p < 0.01).
Mentions: To investigate the correlation between decreased oxidative stress and protein ubiquitination in sch9Δ cells, the concentrations of carbonyl groups in oxidized intracellular proteins in WT and sch9Δ cells were evaluated. In log phase, the level of protein carbonyl in sch9Δ cells was ~30% lower than that in WT cells. Adding Sch9 back restored the level of protein carbonyl to a similar level as that in wild type cells (Fig. 6A).

Bottom Line: In this study, we found that the overall level of ubiquitinated proteins dramatically decreased as yeast cell grew from log to stationary phase.Deletion of SCH9, a gene encoding a key protein kinase for longevity control, decreased the level of ubiquitinated proteins in log phase and this effect could be reversed by restoring Sch9 function.Our results revealed for the first time how Sch9 regulates the level of ubiquitinated proteins and provides new insight into how Sch9 controls longevity.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Bio-Resources and Eco-Environment of Ministry of Education, College of Life Science, Sichuan University, Chengdu, Sichuan 610064, China.

No MeSH data available.


Related in: MedlinePlus