Isolation and characterization of high-osmolarity-sensitive mutants of fission yeast

Hirofumi Aiba, Ryosuke Kawaura, Eiji Yamamoto, Hisami Yamada, Kaoru Takegawa, Takeshi Mizuno

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

For the fission yeast Schizosaccharomyces pombe, adaptation to high- osmolarity medium is mediated by a mitogen-activated protein (MAP) kinase cascade, involving the Wis1 MAP kinase kinase and the Sty1 MAP kinase. The MAP kinase pathway transduces an osmotic signal and accordingly regulates the expression of the downstream target gene (gpd1 + ) that encodes NADH-dependent glycerol-3-phosphate dehydrogenase, in order to adaptively accumulate glycerol inside the cells as an osmoprotectant. We previously characterized a set of high-osmolarity-sensitive S. pombe mutants, including wis1, sty1, and gpd1. In this study, we attempted to further isolate novel osmolarity- sensitive mutants. For some of the mutants isolated, profiles of glycerol production in response to the osmolarity of the growth medium were indistinguishable from that of the wild-type cells, suggesting that they are novel types. They were classified into three distinct types genetically and, thus, were designated hos1, hos2, and hos3 (high osmolarity sensitive) mutants. One of them, the hos1 mutant, was characterized in detail. The hos1 mutant was demonstrated to have a mutational lesion in the known ryh1 + gene, which encodes a small GTP-binding protein. Disruption of the ryh1 + gene results not only in osmosensitivity but also in temperature sensitivity for growth. It was also found that the Δryh1 mutant is severely sterile. These results are discussed with special reference to the osmoadaptation of S. pombe.

Original languageEnglish
Pages (from-to)5038-5043
Number of pages6
JournalJournal of bacteriology
Volume180
Issue number19
Publication statusPublished - Oct 1 1998
Externally publishedYes

Fingerprint

Schizosaccharomyces
Osmolar Concentration
Mitogen-Activated Protein Kinases
Glycerol
Genes
Glycerolphosphate Dehydrogenase
MAP Kinase Kinase Kinases
Mitogen-Activated Protein Kinase Kinases
Growth
GTP-Binding Proteins
NAD
Temperature

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Cite this

Aiba, H., Kawaura, R., Yamamoto, E., Yamada, H., Takegawa, K., & Mizuno, T. (1998). Isolation and characterization of high-osmolarity-sensitive mutants of fission yeast. Journal of bacteriology, 180(19), 5038-5043.

Isolation and characterization of high-osmolarity-sensitive mutants of fission yeast. / Aiba, Hirofumi; Kawaura, Ryosuke; Yamamoto, Eiji; Yamada, Hisami; Takegawa, Kaoru; Mizuno, Takeshi.

In: Journal of bacteriology, Vol. 180, No. 19, 01.10.1998, p. 5038-5043.

Research output: Contribution to journalArticle

Aiba, H, Kawaura, R, Yamamoto, E, Yamada, H, Takegawa, K & Mizuno, T 1998, 'Isolation and characterization of high-osmolarity-sensitive mutants of fission yeast', Journal of bacteriology, vol. 180, no. 19, pp. 5038-5043.
Aiba H, Kawaura R, Yamamoto E, Yamada H, Takegawa K, Mizuno T. Isolation and characterization of high-osmolarity-sensitive mutants of fission yeast. Journal of bacteriology. 1998 Oct 1;180(19):5038-5043.
Aiba, Hirofumi ; Kawaura, Ryosuke ; Yamamoto, Eiji ; Yamada, Hisami ; Takegawa, Kaoru ; Mizuno, Takeshi. / Isolation and characterization of high-osmolarity-sensitive mutants of fission yeast. In: Journal of bacteriology. 1998 ; Vol. 180, No. 19. pp. 5038-5043.
@article{960fc23824c348e59fdfc0c26d2074d7,
title = "Isolation and characterization of high-osmolarity-sensitive mutants of fission yeast",
abstract = "For the fission yeast Schizosaccharomyces pombe, adaptation to high- osmolarity medium is mediated by a mitogen-activated protein (MAP) kinase cascade, involving the Wis1 MAP kinase kinase and the Sty1 MAP kinase. The MAP kinase pathway transduces an osmotic signal and accordingly regulates the expression of the downstream target gene (gpd1 + ) that encodes NADH-dependent glycerol-3-phosphate dehydrogenase, in order to adaptively accumulate glycerol inside the cells as an osmoprotectant. We previously characterized a set of high-osmolarity-sensitive S. pombe mutants, including wis1, sty1, and gpd1. In this study, we attempted to further isolate novel osmolarity- sensitive mutants. For some of the mutants isolated, profiles of glycerol production in response to the osmolarity of the growth medium were indistinguishable from that of the wild-type cells, suggesting that they are novel types. They were classified into three distinct types genetically and, thus, were designated hos1, hos2, and hos3 (high osmolarity sensitive) mutants. One of them, the hos1 mutant, was characterized in detail. The hos1 mutant was demonstrated to have a mutational lesion in the known ryh1 + gene, which encodes a small GTP-binding protein. Disruption of the ryh1 + gene results not only in osmosensitivity but also in temperature sensitivity for growth. It was also found that the Δryh1 mutant is severely sterile. These results are discussed with special reference to the osmoadaptation of S. pombe.",
author = "Hirofumi Aiba and Ryosuke Kawaura and Eiji Yamamoto and Hisami Yamada and Kaoru Takegawa and Takeshi Mizuno",
year = "1998",
month = "10",
day = "1",
language = "English",
volume = "180",
pages = "5038--5043",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "19",

}

TY - JOUR

T1 - Isolation and characterization of high-osmolarity-sensitive mutants of fission yeast

AU - Aiba, Hirofumi

AU - Kawaura, Ryosuke

AU - Yamamoto, Eiji

AU - Yamada, Hisami

AU - Takegawa, Kaoru

AU - Mizuno, Takeshi

PY - 1998/10/1

Y1 - 1998/10/1

N2 - For the fission yeast Schizosaccharomyces pombe, adaptation to high- osmolarity medium is mediated by a mitogen-activated protein (MAP) kinase cascade, involving the Wis1 MAP kinase kinase and the Sty1 MAP kinase. The MAP kinase pathway transduces an osmotic signal and accordingly regulates the expression of the downstream target gene (gpd1 + ) that encodes NADH-dependent glycerol-3-phosphate dehydrogenase, in order to adaptively accumulate glycerol inside the cells as an osmoprotectant. We previously characterized a set of high-osmolarity-sensitive S. pombe mutants, including wis1, sty1, and gpd1. In this study, we attempted to further isolate novel osmolarity- sensitive mutants. For some of the mutants isolated, profiles of glycerol production in response to the osmolarity of the growth medium were indistinguishable from that of the wild-type cells, suggesting that they are novel types. They were classified into three distinct types genetically and, thus, were designated hos1, hos2, and hos3 (high osmolarity sensitive) mutants. One of them, the hos1 mutant, was characterized in detail. The hos1 mutant was demonstrated to have a mutational lesion in the known ryh1 + gene, which encodes a small GTP-binding protein. Disruption of the ryh1 + gene results not only in osmosensitivity but also in temperature sensitivity for growth. It was also found that the Δryh1 mutant is severely sterile. These results are discussed with special reference to the osmoadaptation of S. pombe.

AB - For the fission yeast Schizosaccharomyces pombe, adaptation to high- osmolarity medium is mediated by a mitogen-activated protein (MAP) kinase cascade, involving the Wis1 MAP kinase kinase and the Sty1 MAP kinase. The MAP kinase pathway transduces an osmotic signal and accordingly regulates the expression of the downstream target gene (gpd1 + ) that encodes NADH-dependent glycerol-3-phosphate dehydrogenase, in order to adaptively accumulate glycerol inside the cells as an osmoprotectant. We previously characterized a set of high-osmolarity-sensitive S. pombe mutants, including wis1, sty1, and gpd1. In this study, we attempted to further isolate novel osmolarity- sensitive mutants. For some of the mutants isolated, profiles of glycerol production in response to the osmolarity of the growth medium were indistinguishable from that of the wild-type cells, suggesting that they are novel types. They were classified into three distinct types genetically and, thus, were designated hos1, hos2, and hos3 (high osmolarity sensitive) mutants. One of them, the hos1 mutant, was characterized in detail. The hos1 mutant was demonstrated to have a mutational lesion in the known ryh1 + gene, which encodes a small GTP-binding protein. Disruption of the ryh1 + gene results not only in osmosensitivity but also in temperature sensitivity for growth. It was also found that the Δryh1 mutant is severely sterile. These results are discussed with special reference to the osmoadaptation of S. pombe.

UR - http://www.scopus.com/inward/record.url?scp=0031691307&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031691307&partnerID=8YFLogxK

M3 - Article

VL - 180

SP - 5038

EP - 5043

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 19

ER -