Isolated chloroplast division machinery can actively constrict after stretching

Science. 2006 Sep 8;313(5792):1435-8. doi: 10.1126/science.1129689.

Abstract

Chloroplast division involves plastid-dividing, dynamin, and FtsZ (PDF) rings. We isolated intact supertwisted (or spiral) and circular PDF machineries from chloroplasts of the red alga Cyanidioschyzon merolae. After individual intact PDF machineries were stretched to four times their original lengths with optical tweezers, they spontaneously returned to their original sizes. Dynamin-released PDF machineries did not retain the spiral structure and could not be stretched. Thus, dynamin may generate the motive force for contraction by filament sliding in dividing chloroplasts, in addition to pinching-off the membranes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / physiology*
  • Actin Cytoskeleton / ultrastructure
  • Algal Proteins / physiology*
  • Chloroplasts / physiology*
  • Chloroplasts / ultrastructure
  • Dynamins / physiology*
  • GTP Phosphohydrolases / physiology
  • Intracellular Membranes / physiology
  • Intracellular Membranes / ultrastructure
  • Microscopy, Immunoelectron
  • Rhodophyta / physiology*
  • Rhodophyta / ultrastructure

Substances

  • Algal Proteins
  • GTP Phosphohydrolases
  • Dynamins