Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Stricker, J.; Maddox, P.; Salmon, E D; and Erickson, H. P Proceedings of the National Academy of Sciences of the United States of America, 99(5):3171--3175, March, 2002.
Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching [link]Paper  doi  abstract   bibtex   
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.
@article{stricker_rapid_2002,
	title = {Rapid assembly dynamics of the {Escherichia} coli {FtsZ}-ring demonstrated by fluorescence recovery after photobleaching},
	volume = {99},
	issn = {0027-8424},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/11854462},
	doi = {10.1073/pnas.052595099},
	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.},
	number = {5},
	urldate = {2009-06-23TZ},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	author = {Stricker, Jesse and Maddox, Paul and Salmon, E D and Erickson, Harold P},
	month = mar,
	year = {2002},
	pmid = {11854462},
	keywords = {Bacterial Proteins, Carrier Proteins, Cell Cycle Proteins, Cytoskeletal Proteins, Escherichia coli, Escherichia coli Proteins, Fluorescence, Green Fluorescent Proteins, Luminescent Proteins, Recombinant Fusion Proteins, Time Factors},
	pages = {3171--3175}
}
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