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Updated: Mar 19, 2026

FtsZ Polymerization Assays: Simple Protocols and Considerations
Published on: November 16, 2013
Chloroplast FtsZ assembles into a contractible ring via tubulin-like heteropolymerization
Yamato Yoshida1, Yuko Mogi2, Allan D TerBush1
1Department of Plant Biology, Michigan State University, East Lansing 48824-1312, Michigan, USA.
Abstract:
Chloroplast division is driven by a ring containing FtsZ1 and FtsZ2 proteins, which originated from bacterial FtsZ, a tubulin-like protein; however, mechanistic details of the chloroplast FtsZ ring remain unclear. Here, we report that FtsZ1 and FtsZ2 can heteropolymerize into a contractible ring ex vivo. Fluorescently labelled FtsZ1 and/or FtsZ2 formed single rings in cells of the yeast Pichia pastoris. Photobleaching experiments indicated that co-assembly of FtsZ1 and FtsZ2 imparts polarity to polymerization. Assembly of FtsZ chimaeras revealed that the protofilaments assemble via heteropolymerization of FtsZ2 and FtsZ1. Contraction of the ring was accompanied by an increase in the filament turnover rate. Our findings suggest that the evolutionary duplication of FtsZ in plants may have increased the mobility and kinetics of FtsZ ring dynamics in chloroplast division. Thus, the gene duplication and heteropolymerization of chloroplast FtsZs may represent convergent evolution with eukaryotic tubulin.
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