Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain.
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.
Ohashi
Tomoo
T
Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710-3709, USA.
Hale
Cynthia A
CA
de Boer
Piet A J
PA
Erickson
Harold P
HP
D001426:Bacterial Proteins / Q000737:chemistry* / Q000648:ultrastructure; D002352:Carrier Proteins / Q000737:chemistry* / Q000648:ultrastructure; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000648:ultrastructure; D002455:Cell Division; D003598:Cytoskeletal Proteins; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D005973:Glutamine / Q000737:chemistry; D049452:Green Fluorescent Proteins; D008164:Luminescent Proteins; D008854:Microscopy, Electron; D008958:Models, Molecular; D011392:Proline / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation
D001426:Bacterial Proteins; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C071525:FtsZ protein, Bacteria; D008164:Luminescent Proteins; C103795:ZipA protein, E coli; D005973:Glutamine; D049452:Green Fluorescent Proteins; D011392:Proline