ALERT: This system is being upgraded on Tuesday December 12. It will not be available
for use for several hours that day while the upgrade is in progress. Deposits to DukeSpace
will be disabled on Monday December 11, so no new items are to be added to the repository
while the upgrade is in progress. Everything should be back to normal by the end of
day, December 12.
The cell division protein MinD from Pseudomonas aeruginosa dominates the assembly of the MinC-MinD copolymers.
Abstract
Cell division of rod-shaped bacteria requires the Z ring, a ring of FtsZ filaments
associated with the inner-membrane wall. The MinCDE proteins help localize the Z ring
to the center of the Escherichia coli cell. MinC, which inhibits Z-ring assembly,
is a passenger on MinD. Previous studies have shown that MinC-MinD from E. coli and
Aquifex aeolicus assemble in vitro into extended filaments with a 1:1 stoichiometry.
However, a recent study has raised questions about the function of the MinC-MinD copolymer
in vivo, since its assembly appears to require a high concentration of these two proteins,
has a long lag time, and its blockade does not affect in vivo activities. Here, we
found that MinC and MinD from Pseudomonas aeruginosa coassemble into filaments with
a 1:1 stoichiometry. We also found that the minimal concentration of ~4 μM required
for assembly applies only to MinD because above 4 μM MinD, even very low MinC concentrations
sustained coassembly. As previously reported, the MinC-MinD coassembly exhibited a
long lag of ~100 s when initiated by ATP. Premixing MinD with ATP eliminated this
lag, suggesting that it may be due to slow MinD dimerization following ATP activation.
We also discovered that MinC-MinD copolymers quickly bound and formed huge bundles
with FtsZ filaments. Our results resolve previous questions about the low concentration
of MinC and the lag time, insights that may inform future investigations into the
exact role of the MinC-MinD copolymer in vivo.
Type
Journal articleSubject
FtsZMinC-MinD copolymer
MinCDE proteins
Z-ring
bacteria
cell division
cytoskeleton
electron microscopy (EM)
min system
protein dynamic
Permalink
https://hdl.handle.net/10161/16623Published Version (Please cite this version)
10.1074/jbc.ra117.001513Publication Info
Huang, Haiyan; Wang, Ping; Bian, Li; Osawa, Masaki; Erickson, Harold P; & Chen, Yaodong (2018). The cell division protein MinD from Pseudomonas aeruginosa dominates the assembly
of the MinC-MinD copolymers. The Journal of biological chemistry. 10.1074/jbc.ra117.001513. Retrieved from https://hdl.handle.net/10161/16623.This is constructed from limited available data and may be imprecise. To cite this
article, please review & use the official citation provided by the journal.
Collections
More Info
Show full item recordScholars@Duke
Harold Paul Erickson
James B. Duke Distinguished Professor Emeritus
Recent research has been on cytoskeleton (eukaryotes and bacteria); a skirmish to
debunk the irisin story; a reinterpretation of proposed multivalent binders of the
coronavirus spike protein. I have also published an ebook on "Principles of Protein-Protein
Association" suitable for a course module or individual learning.
Masaki Osawa
Assistant Research Professor of Cell Biology
Alphabetical list of authors with Scholars@Duke profiles.

Articles written by Duke faculty are made available through the campus open access policy. For more information see: Duke Open Access Policy
Rights for Collection: Scholarly Articles
Works are deposited here by their authors, and represent their research and opinions, not that of Duke University. Some materials and descriptions may include offensive content. More info