Related Experiment Video
Updated: Aug 1, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
Published on: July 30, 2014
A defect in a fatty acyl-CoA synthetase gene, lcf1+, results in a decrease in viability after entry into the
1Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, 464-8601 Nagoya, Japan.
A Schizosaccharomyces pombe mutant lacking the lcf1+ gene rapidly loses viability in stationary phase. This long-chain fatty acyl-CoA synthetase is crucial for cell survival under stress conditions.
Area of Science:
- Cellular Biology
- Molecular Genetics
- Biochemistry
Background:
- Schizosaccharomyces pombe is a model organism for studying eukaryotic cell biology.
- Cellular viability during stationary phase is critical for microbial survival.
- Long-chain fatty acyl-CoA synthetases are enzymes involved in lipid metabolism.
Purpose of the Study:
- To investigate the function of the lcf1+ gene in Schizosaccharomyces pombe.
- To characterize a mutant defective in stationary phase viability.
- To understand the role of long-chain fatty acyl-CoA synthetase in cellular stress response.
Main Methods:
- Isolation and characterization of a Schizosaccharomyces pombe mutant.
- Phenotypic analysis including viability assays, temperature sensitivity, and salt tolerance.
- Gene identification through mutational lesion analysis.
- Homology comparison with related genes in Saccharomyces cerevisiae.
Main Results:
- A mutant defective in stationary phase viability was identified.
- The defect was mapped to a mutation in the lcf1+ gene, encoding a long-chain fatty acyl-CoA synthetase.
- The lcf1Δ mutant exhibited sensitivity to high temperature (37°C) and high salt concentrations (0.9 M KCl).
- The mutant cells grew normally during the logarithmic phase but rapidly lost viability upon entering stationary phase.
Conclusions:
- The lcf1+ gene is essential for maintaining viability in stationary phase in Schizosaccharomyces pombe.
- Lcf1p likely plays a role in managing endogenous acyl-CoA pools, contributing to stress tolerance.
- The findings suggest a conserved function of long-chain fatty acyl-CoA synthetases in cellular homeostasis and stress response across yeast species.
More Related Videos
07:55A Deep-sequencing-assisted, Spontaneous Suppressor Screen in the Fission Yeast Schizosaccharomyces pombe
Published on: March 7, 2019
08:07Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe
Published on: May 2, 2025
Related Concept Videos
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Lethal Alleles
Lucien Cuénot discovered lethal alleles in 1905 while studying the inheritance of coat color in mice. The agouti gene is responsible for the color of the coat in mice. This gene codes for an agouti-signaling protein, which is responsible for melanin distribution in mammals. The wild-type allele gives rise to gray-brown coat color in mice, while the mutant allele gives rise to yellow coat color. In addition to coat color, the agouti gene is associated with the yellow...
Overview of Fatty Acid Metabolism
Fatty acids are catabolized in a process called beta-oxidation, which takes place in the matrix of the mitochondria and converts their fatty acid chains into two-carbon units of acetyl groups. The acetyl...
Gene Regulation During Sporulation