Abstract
Phosphatidylinositol (PI) 3-kinase (encoded by the pik3+ gene) in Schizosaccharomyces pombe has been identified as a homologue of VPS34p, a protein required for proper vesicular protein sorting. The clone defective in this protein carries enlarged vacuoles and exhibits sensitivity to high temperature or high ion concentration. The effect of disruption of pik3+ on sporulation of Sz. pombe was examined. The diploid cells underwent G1 arrest and meiosis. However, the spores formed by the Δpik3 cells were not viable. Electron-microscopic analysis revealed that the growth of the forespore membrane of Δpik3 cells was not correctly orientated, failing to engulf the nucleus or forming extremely small spores, as was confirmed by the use of Spo3p-GFP and GFP-Psy1p, which are markers of the forespore membrane. The coating materials found along the forespore membrane of the wild-type were greatly reduced in these cells. PI 3-P, the product of Pik3p, was detected on the forespore membrane, suggesting that PI 3-P-dependent vesicle transport may take place in formation of the forespore membrane. Misshaped forespore membrane, accumulation of vesicles, formation of small non-viable spores, and suppression by over expression of Psy1p were the phenotypes commonly seen in Δpik3 and Δspo3 cells, suggesting a relationship between the functions of Pik3p and Spo3p in formation of the forespore membrane in Sz. pombe.
| Original language | English |
|---|---|
| Pages (from-to) | 193-206 |
| Number of pages | 14 |
| Journal | Yeast |
| Volume | 20 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Feb 1 2003 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Bioengineering
- Biochemistry
- Applied Microbiology and Biotechnology
- Genetics
Cite this
Role of phosphatidylinositol 3-phosphate in formation of forespore membrane in Schizosaccharomyces pombe. / Onishi, Masayuki; Koga, Takako; Morita, Rika; Nakamura, Yoko; Nakamura, Taro; Shimoda, Chikashi; Takegawa, Kaoru; Hirata, Aiko; Fukui, Yasuhisa.
In: Yeast, Vol. 20, No. 3, 01.02.2003, p. 193-206.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Role of phosphatidylinositol 3-phosphate in formation of forespore membrane in Schizosaccharomyces pombe
AU - Onishi, Masayuki
AU - Koga, Takako
AU - Morita, Rika
AU - Nakamura, Yoko
AU - Nakamura, Taro
AU - Shimoda, Chikashi
AU - Takegawa, Kaoru
AU - Hirata, Aiko
AU - Fukui, Yasuhisa
PY - 2003/2/1
Y1 - 2003/2/1
N2 - Phosphatidylinositol (PI) 3-kinase (encoded by the pik3+ gene) in Schizosaccharomyces pombe has been identified as a homologue of VPS34p, a protein required for proper vesicular protein sorting. The clone defective in this protein carries enlarged vacuoles and exhibits sensitivity to high temperature or high ion concentration. The effect of disruption of pik3+ on sporulation of Sz. pombe was examined. The diploid cells underwent G1 arrest and meiosis. However, the spores formed by the Δpik3 cells were not viable. Electron-microscopic analysis revealed that the growth of the forespore membrane of Δpik3 cells was not correctly orientated, failing to engulf the nucleus or forming extremely small spores, as was confirmed by the use of Spo3p-GFP and GFP-Psy1p, which are markers of the forespore membrane. The coating materials found along the forespore membrane of the wild-type were greatly reduced in these cells. PI 3-P, the product of Pik3p, was detected on the forespore membrane, suggesting that PI 3-P-dependent vesicle transport may take place in formation of the forespore membrane. Misshaped forespore membrane, accumulation of vesicles, formation of small non-viable spores, and suppression by over expression of Psy1p were the phenotypes commonly seen in Δpik3 and Δspo3 cells, suggesting a relationship between the functions of Pik3p and Spo3p in formation of the forespore membrane in Sz. pombe.
AB - Phosphatidylinositol (PI) 3-kinase (encoded by the pik3+ gene) in Schizosaccharomyces pombe has been identified as a homologue of VPS34p, a protein required for proper vesicular protein sorting. The clone defective in this protein carries enlarged vacuoles and exhibits sensitivity to high temperature or high ion concentration. The effect of disruption of pik3+ on sporulation of Sz. pombe was examined. The diploid cells underwent G1 arrest and meiosis. However, the spores formed by the Δpik3 cells were not viable. Electron-microscopic analysis revealed that the growth of the forespore membrane of Δpik3 cells was not correctly orientated, failing to engulf the nucleus or forming extremely small spores, as was confirmed by the use of Spo3p-GFP and GFP-Psy1p, which are markers of the forespore membrane. The coating materials found along the forespore membrane of the wild-type were greatly reduced in these cells. PI 3-P, the product of Pik3p, was detected on the forespore membrane, suggesting that PI 3-P-dependent vesicle transport may take place in formation of the forespore membrane. Misshaped forespore membrane, accumulation of vesicles, formation of small non-viable spores, and suppression by over expression of Psy1p were the phenotypes commonly seen in Δpik3 and Δspo3 cells, suggesting a relationship between the functions of Pik3p and Spo3p in formation of the forespore membrane in Sz. pombe.
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UR - http://www.scopus.com/inward/citedby.url?scp=0037326461&partnerID=8YFLogxK
U2 - 10.1002/yea.953
DO - 10.1002/yea.953
M3 - Review article
C2 - 12557273
AN - SCOPUS:0037326461
VL - 20
SP - 193
EP - 206
JO - Yeast
JF - Yeast
SN - 0749-503X
IS - 3
ER -