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Rapid in vitro assembly of Caulobacter crescentus FtsZ protein at pH 6.5 and 7.2.

dc.contributor.author Erickson, Harold Paul
dc.contributor.author Milam, Sara L
dc.date.accessioned 2018-04-01T14:48:11Z
dc.date.available 2018-04-01T14:48:11Z
dc.date.issued 2013-08
dc.identifier.issn 1083-351X
dc.identifier.issn 1083-351X
dc.identifier.uri https://hdl.handle.net/10161/16453
dc.description.abstract FtsZ from most bacteria assembles rapidly in vitro, reaching a steady-state plateau in 5-10 s after addition of GTP. A recent study used a novel dynamic light-scattering technique to assay the assembly of FtsZ from Caulobacter crescentus (CcFtsZ) and reported that assembly required 10 min, ∼100 times slower than for related bacteria. Previous studies had indicated normal, rapid assembly of CcFtsZ. We have reinvestigated the assembly kinetics using a mutant L72W, where assembly of subunits into protofilaments results in a significant increase in tryptophan fluorescence. We found that assembly reached a plateau in 5-10 s and showed no change in the following 10 min. This was confirmed by 90° light scattering and negative-stain electron microscopy. The very slow kinetics in the dynamic light-scattering study may be related to a refractory state induced when the FtsZ protein is stored without nucleotide, a phenomenon that we had observed in a previous study of EcFtsZ. We conclude that CcFtsZ is not an outlier, but shows rapid assembly kinetics similar to FtsZ from related bacteria.
dc.language eng
dc.relation.ispartof The Journal of biological chemistry
dc.relation.isversionof 10.1074/jbc.m113.491845
dc.subject Caulobacter crescentus
dc.subject Magnesium
dc.subject GTP Phosphohydrolases
dc.subject Bacterial Proteins
dc.subject Cytoskeletal Proteins
dc.subject Guanosine Triphosphate
dc.subject Negative Staining
dc.subject Hydrolysis
dc.subject Kinetics
dc.subject Hydrogen-Ion Concentration
dc.subject Fluorescence
dc.subject Scattering, Radiation
dc.title Rapid in vitro assembly of Caulobacter crescentus FtsZ protein at pH 6.5 and 7.2.
dc.type Journal article
dc.date.updated 2018-04-01T14:48:10Z
pubs.issue 33
pubs.organisational-group School of Medicine
pubs.organisational-group Duke
pubs.organisational-group Duke Cancer Institute
pubs.organisational-group Institutes and Centers
pubs.organisational-group Biochemistry
pubs.organisational-group Basic Science Departments
pubs.organisational-group Cell Biology
pubs.publication-status Published
pubs.volume 288


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