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An evolutionary puzzle: chloroplast and mitochondrial division rings

Shin-ya Miyagishima1, Keiji Nishida, Tsuneyoshi Kuroiwa

  • 1Department of Life Science, College of Science, Rikkyo (St Paul's) University, 3-34-1 Nishiikebukuro, Toshima-ku, Tokyo 171-8501, Japan. z2002376@rikkyo.ne.jp

Trends in Plant Science
|September 19, 2003
PubMed

Insights

Chloroplast and mitochondria division involves bacterial FtsZ rings and distinct eukaryote-specific dynamin-related GTPase rings. This suggests a hybrid system for organelle division, merging bacterial and eukaryotic components.

Area of Science:

  • Cell Biology
  • Organelle Biology
  • Evolutionary Biology

Background:

  • Chloroplasts and mitochondria, originating from bacteria, retain FtsZ rings for division.
  • Organelle division machinery has evolved, losing bacterial proteins but gaining new components.
  • Eukaryote-specific dynamin-related GTPases regulate organelle division.

Purpose of the Study:

  • To investigate the division mechanisms of chloroplasts and primitive mitochondria.
  • To understand the roles of FtsZ rings and dynamin-related GTPases in organelle division.
  • To elucidate the evolutionary origins of organelle division systems.

Main Methods:

  • Comparative analysis of protein homologues across different species.
  • Investigation of FtsZ ring and plastid/mitochondrion dividing ring functions.
  • Study of dynamin-related GTPase involvement in chloroplast and mitochondrial division.

Main Results:

  • Chloroplasts and mitochondria utilize both FtsZ rings and distinct organelle-specific dividing rings.
  • Eukaryote-specific dynamin-related GTPases are crucial for regulating organelle division.
  • These division systems appear conserved early in eukaryotic evolution.

Conclusions:

  • Organelle division in eukaryotes involves a hybrid system.
  • This system combines bacterial-derived components (FtsZ) with eukaryote-specific proteins (dynamin-related GTPases).
  • The division machinery for chloroplasts and primitive mitochondria is remarkably similar.

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