Related Experiment Video

Updated: Aug 14, 2026

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae
08:55

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae

Published on: July 19, 2021

Fredericamycin A affects mitochondrial inheritance and morphology in Saccharomyces cerevisiae

Yuko Imamura1, Masashi Yukawa, Ken-ichi Kimura

  • 1Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Japan.

Bioscience, Biotechnology, and Biochemistry
|November 25, 2005
PubMed

Insights

Fredericamycin A (FMA), an antibiotic from Streptomyces griseus, induces G1 cell cycle arrest in yeast. This study reveals mitochondria as the primary target of FMA, impacting cell growth and drug resistance.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Fredericamycin A (FMA) is an antibiotic produced by Streptomyces griseus.
  • FMA demonstrates modest antitumor activity but its in vivo mechanisms remain unclear.
  • Previous research suggested topoisomerase I as a potential FMA target.

Purpose of the Study:

  • To elucidate the in vivo functions and cellular targets of Fredericamycin A.
  • To investigate FMA's effect on cell cycle progression and mitochondrial function.
  • To determine the relationship between drug resistance and FMA's mechanism of action.

Main Methods:

  • Utilized Saccharomyces cerevisiae as a model organism.
  • Assessed FMA's impact on cell cycle (G1 arrest) and cytotoxicity (IC50).
  • Examined mitochondrial morphology (aggregation, petite induction) and FMA resistance in rho(-) vs. rho(+) cells.
  • Investigated the role of topoisomerase I overexpression in FMA sensitivity.

Main Results:

  • FMA was identified as an inducer of G1 arrest in yeast.
  • FMA exhibited potent cytotoxicity (IC50 = 24 nM) against W303-MLC30 cells.
  • FMA rapidly induced mitochondrial aggregation and petite formation.
  • Mitochondrial dysfunction correlated with increased FMA resistance; rho(-) cells were significantly more resistant than rho(+) cells.
  • Overexpression of topoisomerase I did not mitigate FMA's effects.

Conclusions:

  • Mitochondria are identified as the primary cellular target of Fredericamycin A.
  • FMA's mechanism involves mitochondrial disruption, leading to cell cycle arrest and cytotoxicity.
  • Drug resistance is linked to mitochondrial integrity and function, not topoisomerase I activity.

More Related Videos

A high-throughput method to globally study the organelle morphology in S. cerevisiae07:29

A high-throughput method to globally study the organelle morphology in S. cerevisiae

Published on: March 2, 2009

Fission Yeast as a Platform for Antibacterial Drug Screens Targeting Bacterial Cytoskeleton Proteins05:57

Fission Yeast as a Platform for Antibacterial Drug Screens Targeting Bacterial Cytoskeleton Proteins

Published on: April 26, 2024

Related Concept Videos

Animal Mitochondrial Genetics02:59

Animal Mitochondrial Genetics

Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
Inhibitors of Bacterial Protein Synthesis01:25

Inhibitors of Bacterial Protein Synthesis

Aminoglycosides constitute a highly potent class of bactericidal antibiotics that exert their antimicrobial effects by targeting the bacterial ribosome, specifically disrupting protein synthesis. These polycationic molecules consist of amino-modified sugars linked via glycosidic bonds to an aminocyclitol core such as 2-deoxystreptamine or streptamine. Their strong positive charges facilitate tight binding to the negatively charged phosphate backbone of ribosomal RNA (rRNA), primarily at the 16S...