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
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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.
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Show full item recordScholars@Duke
Harold Paul Erickson
James B. Duke Distinguished Professor of Cell Biology
Cytoskeleton: It is now clear that the actin and microtubule cytoskeleton originated
in bacteria. Our major research is on FtsZ, the bacterial tubulin homolog, which assembles
into a contractile ring that divides the bacterium. We have studied FtsZ assembly
in vitro, and found that it assembles into thin protofilaments (pfs). Dozens of these
pfs are further clustered to form the contractile Z-ring in vivo. Some important discoveries
in the last ten years include:
&bul
Masaki Osawa
Assistant Research Professor of Cell Biology
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