The cell division protein MinD from Pseudomonas aeruginosa dominates the assembly of the MinC-MinD copolymers.
| dc.contributor.author | Huang, Haiyan | |
| dc.contributor.author | Wang, Ping | |
| dc.contributor.author | Bian, Li | |
| dc.contributor.author | Osawa, Masaki | |
| dc.contributor.author | Erickson, Harold P | |
| dc.contributor.author | Chen, Yaodong | |
| dc.date.accessioned | 2018-05-01T13:22:05Z | |
| dc.date.available | 2018-05-01T13:22:05Z | |
| dc.date.issued | 2018-04-02 | |
| dc.date.updated | 2018-05-01T13:22:03Z | |
| dc.description.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. | |
| dc.identifier.issn | 0021-9258 | |
| dc.identifier.issn | 1083-351X | |
| dc.identifier.uri | ||
| dc.language | eng | |
| dc.publisher | Elsevier BV | |
| dc.relation.ispartof | The Journal of biological chemistry | |
| dc.relation.isversionof | 10.1074/jbc.ra117.001513 | |
| dc.subject | FtsZ | |
| dc.subject | MinC-MinD copolymer | |
| dc.subject | MinCDE proteins | |
| dc.subject | Z-ring | |
| dc.subject | bacteria | |
| dc.subject | cell division | |
| dc.subject | cytoskeleton | |
| dc.subject | electron microscopy (EM) | |
| dc.subject | min system | |
| dc.subject | protein dynamic | |
| dc.title | The cell division protein MinD from Pseudomonas aeruginosa dominates the assembly of the MinC-MinD copolymers. | |
| dc.type | Journal article | |
| duke.contributor.orcid | Erickson, Harold P|0000-0002-9104-8987 | |
| 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 |