PMID:11854462
| Citation |
Stricker, J, Maddox, P, Salmon, ED and Erickson, HP (2002) Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc. Natl. Acad. Sci. U.S.A. 99:3171-5 |
|---|---|
| Abstract |
FtsZ, the major cytoskeletal component of the bacterial cell-division machine, assembles into a ring (the Z-ring) that contracts at septation. FtsZ is a bacterial homolog of tubulin, with similar tertiary structure, GTP hydrolysis, and in vitro assembly. We used green fluorescent protein-labeled FtsZ and fluorescence recovery after photobleaching to show that the E. coli Z-ring is extremely dynamic, continually remodeling itself with a half-time of 30 s. ZipA, a membrane protein involved in cell division that colocalizes with FtsZ, was equally dynamic. The Z-ring of the mutant ftsZ84, which has 1/10 the guanosine triphosphatase activity of wild-type FtsZ in vitro, showed a 9-fold slower turnover in vivo. This finding implies that assembly dynamics are determined primarily by GTP hydrolysis. Despite the greatly reduced assembly dynamics, the ftsZ84 cells divide with a normal cell-cycle time. |
| Links |
PubMed PMC122491 Online version:10.1073/pnas.052595099 |
| Keywords |
Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Carrier Proteins/metabolism; Cell Cycle Proteins/metabolism; Cytoskeletal Proteins; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Fluorescence; Green Fluorescent Proteins; Luminescent Proteins/genetics; Luminescent Proteins/metabolism; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Time Factors |
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