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Updated: Sep 30, 2026

FtsZ Polymerization Assays: Simple Protocols and Considerations
Published on: November 16, 2013
Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the
Tomoo Ohashi1, Cynthia A Hale, Piet A J de Boer
1Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710-3709, USA.
Abstract:
The cell division protein ZipA has an N-terminal transmembrane domain and a C-terminal globular domain that binds FtsZ. Between them are a charged domain and a P/Q domain rich in proline and glutamine that has been proposed to be an unfolded polypeptide. Here we provide evidence obtained by electron microscopy that the P/Q domain is a flexible tether ranging in length from 8 to 20 nm and invisible in rotary shadowing electron microscopy. We estimated a persistence length of 0.66 nm, which is similar to the persistence lengths of other unfolded and unstructured polypeptides.
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