Abstract
The GDI1 protein related vesicle transport system was studied to investigate the possibility that an exclusion of toxic zinc (Zn) from the cytoplasm ameliorates Zn toxicity in Saccharomyces cerevisiae (yeast). A temperature-sensitive gdi1 mutant (originally called sec19), in which the GDP dissociation inhibitor becomes inactive at the non-permissive temperature (37°C), was more sensitive to Zn than its parental GDI1 strain at 32°C (a moderately non-permissive temperature). The relative efflux of cytoplasmic Zn in the gdi1 mutant was lower than that in the control strain. Treatment with a vesicle transport-specific inhibitor, Brefeldin A, caused an increase of Zn sensitivity and a decrease of Zn efflux in these strains. It is therefore suggested that the GDI1-related vesicle transport system contributes to Zn tolerance in yeast. Furthermore, changes in the number of Zn-specific fluorescent granules (zincosomes) were observed by zinquin staining in the mutant cells under Zn treatment at 32°C and 37°C. We concluded that the GDI1 protein is implicated in control of vesicle numbers. Collectively, the results suggest that the GDI1protein is involved in Zn efflux via small vesicle trafficking and contributes to the control of cytoplasmic Zn content, allowing yeast to survive in the presence of toxic Zn.
| Original language | English |
|---|---|
| Pages (from-to) | 17-24 |
| Number of pages | 8 |
| Journal | Yeast |
| Volume | 29 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Jan 2012 |
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Keywords
- Exocytosis
- GDP dissociation inhibitor (GDI) protein
- Heavy metal stress
- sec19 mutation
- Vesicle trafficking
- Zinc-specific fluorescent granule
ASJC Scopus subject areas
- Biochemistry
- Biotechnology
- Genetics
- Bioengineering
- Applied Microbiology and Biotechnology
Cite this
Possible involvement of GDI1 protein, a GDP dissociation inhibitor related to vesicle transport, in an amelioration of zinc toxicity in Saccharomyces cerevisiae. / Ezaki, Bunichi; Nakakihara, Eri.
In: Yeast, Vol. 29, No. 1, 01.2012, p. 17-24.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Possible involvement of GDI1 protein, a GDP dissociation inhibitor related to vesicle transport, in an amelioration of zinc toxicity in Saccharomyces cerevisiae
AU - Ezaki, Bunichi
AU - Nakakihara, Eri
PY - 2012/1
Y1 - 2012/1
N2 - The GDI1 protein related vesicle transport system was studied to investigate the possibility that an exclusion of toxic zinc (Zn) from the cytoplasm ameliorates Zn toxicity in Saccharomyces cerevisiae (yeast). A temperature-sensitive gdi1 mutant (originally called sec19), in which the GDP dissociation inhibitor becomes inactive at the non-permissive temperature (37°C), was more sensitive to Zn than its parental GDI1 strain at 32°C (a moderately non-permissive temperature). The relative efflux of cytoplasmic Zn in the gdi1 mutant was lower than that in the control strain. Treatment with a vesicle transport-specific inhibitor, Brefeldin A, caused an increase of Zn sensitivity and a decrease of Zn efflux in these strains. It is therefore suggested that the GDI1-related vesicle transport system contributes to Zn tolerance in yeast. Furthermore, changes in the number of Zn-specific fluorescent granules (zincosomes) were observed by zinquin staining in the mutant cells under Zn treatment at 32°C and 37°C. We concluded that the GDI1 protein is implicated in control of vesicle numbers. Collectively, the results suggest that the GDI1protein is involved in Zn efflux via small vesicle trafficking and contributes to the control of cytoplasmic Zn content, allowing yeast to survive in the presence of toxic Zn.
AB - The GDI1 protein related vesicle transport system was studied to investigate the possibility that an exclusion of toxic zinc (Zn) from the cytoplasm ameliorates Zn toxicity in Saccharomyces cerevisiae (yeast). A temperature-sensitive gdi1 mutant (originally called sec19), in which the GDP dissociation inhibitor becomes inactive at the non-permissive temperature (37°C), was more sensitive to Zn than its parental GDI1 strain at 32°C (a moderately non-permissive temperature). The relative efflux of cytoplasmic Zn in the gdi1 mutant was lower than that in the control strain. Treatment with a vesicle transport-specific inhibitor, Brefeldin A, caused an increase of Zn sensitivity and a decrease of Zn efflux in these strains. It is therefore suggested that the GDI1-related vesicle transport system contributes to Zn tolerance in yeast. Furthermore, changes in the number of Zn-specific fluorescent granules (zincosomes) were observed by zinquin staining in the mutant cells under Zn treatment at 32°C and 37°C. We concluded that the GDI1 protein is implicated in control of vesicle numbers. Collectively, the results suggest that the GDI1protein is involved in Zn efflux via small vesicle trafficking and contributes to the control of cytoplasmic Zn content, allowing yeast to survive in the presence of toxic Zn.
KW - Exocytosis
KW - GDP dissociation inhibitor (GDI) protein
KW - Heavy metal stress
KW - sec19 mutation
KW - Vesicle trafficking
KW - Zinc-specific fluorescent granule
UR - http://www.scopus.com/inward/record.url?scp=84855659625&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84855659625&partnerID=8YFLogxK
U2 - 10.1002/yea.1913
DO - 10.1002/yea.1913
M3 - Article
C2 - 22125264
AN - SCOPUS:84855659625
VL - 29
SP - 17
EP - 24
JO - Yeast
JF - Yeast
SN - 0749-503X
IS - 1
ER -