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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

The level of ubiquitinated proteins during cell growth is regulated by Sch9. (A) The levels of ubiquitinated proteins in WT cells (TB50a) at indicated times after inoculation were tested by western blotting with actin as the loading control. The expression of Sch9 was also detected. (B) The quantifications of three repeats from panel A together with the related cell growth curve estimated by the change of cell concentration. (C) The levels of ubiquitinated proteins in WT cells (TB50a) transformed with empty vector (WT+vector) and Sch9 deletion mutant cells (TS120-2d) transformed with empty vector (sch9Δ+vector) or pRS416−SCH9 (sch9Δ+Sch9) at indicated growth stages were tested by western blotting. L: Log phase at 12–16 h after inoculation (OD600 nm=0.5), S1: Stationary phase at 72 h after inoculation (OD600 nm=8–9), S2: Stationary phase at 120 h after inoculation (OD600 nm=8–9). (D) The quantifications of three repeats from panel C. (*P represents<0.05 and “ns” denotes no significance p>0.05 between the indicated comparisons.).
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f0005: The level of ubiquitinated proteins during cell growth is regulated by Sch9. (A) The levels of ubiquitinated proteins in WT cells (TB50a) at indicated times after inoculation were tested by western blotting with actin as the loading control. The expression of Sch9 was also detected. (B) The quantifications of three repeats from panel A together with the related cell growth curve estimated by the change of cell concentration. (C) The levels of ubiquitinated proteins in WT cells (TB50a) transformed with empty vector (WT+vector) and Sch9 deletion mutant cells (TS120-2d) transformed with empty vector (sch9Δ+vector) or pRS416−SCH9 (sch9Δ+Sch9) at indicated growth stages were tested by western blotting. L: Log phase at 12–16 h after inoculation (OD600 nm=0.5), S1: Stationary phase at 72 h after inoculation (OD600 nm=8–9), S2: Stationary phase at 120 h after inoculation (OD600 nm=8–9). (D) The quantifications of three repeats from panel C. (*P represents<0.05 and “ns” denotes no significance p>0.05 between the indicated comparisons.).

Mentions: When yeast cells are cultured in rich medium (YPD), growth progress from log phase, where cells divide every ~90 min, through the diauxic shift to stationary phase where division ceases [39–41]. Dramatic changes of cellular events occur during the transition from log phase to stationary phase, including the dynamics of ubiquitinated proteins (Fig. 1A, B and S1). When wild type (WT) cells entered to diauxic phase 24 h after inoculation, the overall protein ubiquitination level dropped more than 50% and did not decrease further during the stationary phase (Fig. 1A –C).


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)

The level of ubiquitinated proteins during cell growth is regulated by Sch9. (A) The levels of ubiquitinated proteins in WT cells (TB50a) at indicated times after inoculation were tested by western blotting with actin as the loading control. The expression of Sch9 was also detected. (B) The quantifications of three repeats from panel A together with the related cell growth curve estimated by the change of cell concentration. (C) The levels of ubiquitinated proteins in WT cells (TB50a) transformed with empty vector (WT+vector) and Sch9 deletion mutant cells (TS120-2d) transformed with empty vector (sch9Δ+vector) or pRS416−SCH9 (sch9Δ+Sch9) at indicated growth stages were tested by western blotting. L: Log phase at 12–16 h after inoculation (OD600 nm=0.5), S1: Stationary phase at 72 h after inoculation (OD600 nm=8–9), S2: Stationary phase at 120 h after inoculation (OD600 nm=8–9). (D) The quantifications of three repeats from panel C. (*P represents<0.05 and “ns” denotes no significance p>0.05 between the indicated comparisons.).
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Related In: Results  -  Collection

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f0005: The level of ubiquitinated proteins during cell growth is regulated by Sch9. (A) The levels of ubiquitinated proteins in WT cells (TB50a) at indicated times after inoculation were tested by western blotting with actin as the loading control. The expression of Sch9 was also detected. (B) The quantifications of three repeats from panel A together with the related cell growth curve estimated by the change of cell concentration. (C) The levels of ubiquitinated proteins in WT cells (TB50a) transformed with empty vector (WT+vector) and Sch9 deletion mutant cells (TS120-2d) transformed with empty vector (sch9Δ+vector) or pRS416−SCH9 (sch9Δ+Sch9) at indicated growth stages were tested by western blotting. L: Log phase at 12–16 h after inoculation (OD600 nm=0.5), S1: Stationary phase at 72 h after inoculation (OD600 nm=8–9), S2: Stationary phase at 120 h after inoculation (OD600 nm=8–9). (D) The quantifications of three repeats from panel C. (*P represents<0.05 and “ns” denotes no significance p>0.05 between the indicated comparisons.).
Mentions: When yeast cells are cultured in rich medium (YPD), growth progress from log phase, where cells divide every ~90 min, through the diauxic shift to stationary phase where division ceases [39–41]. Dramatic changes of cellular events occur during the transition from log phase to stationary phase, including the dynamics of ubiquitinated proteins (Fig. 1A, B and S1). When wild type (WT) cells entered to diauxic phase 24 h after inoculation, the overall protein ubiquitination level dropped more than 50% and did not decrease further during the stationary phase (Fig. 1A –C).

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