Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Stricker, J., Maddox, P., Salmon, E D, & Erickson, H. P Proceedings of the National Academy of Sciences of the United States of America, 99(5):3171--3175, March, 2002. 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}
}
Downloads: 0
{"_id":"eCXJa8s5Kryd42hAE","bibbaseid":"stricker-maddox-salmon-erickson-rapidassemblydynamicsoftheescherichiacoliftszringdemonstratedbyfluorescencerecoveryafterphotobleaching-2002","downloads":0,"creationDate":"2017-04-04T08:13:36.090Z","title":"Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching","author_short":["Stricker, J.","Maddox, P.","Salmon, E D","Erickson, H. P"],"year":2002,"bibtype":"article","biburl":"http://bibbase.org/zotero/velocityhughes","bibdata":{"bibtype":"article","type":"article","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":[{"propositions":[],"lastnames":["Stricker"],"firstnames":["Jesse"],"suffixes":[]},{"propositions":[],"lastnames":["Maddox"],"firstnames":["Paul"],"suffixes":[]},{"propositions":[],"lastnames":["Salmon"],"firstnames":["E","D"],"suffixes":[]},{"propositions":[],"lastnames":["Erickson"],"firstnames":["Harold","P"],"suffixes":[]}],"month":"March","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","bibtex":"@article{stricker_rapid_2002,\n\ttitle = {Rapid assembly dynamics of the {Escherichia} coli {FtsZ}-ring demonstrated by fluorescence recovery after photobleaching},\n\tvolume = {99},\n\tissn = {0027-8424},\n\turl = {http://www.ncbi.nlm.nih.gov/pubmed/11854462},\n\tdoi = {10.1073/pnas.052595099},\n\tabstract = {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.},\n\tnumber = {5},\n\turldate = {2009-06-23TZ},\n\tjournal = {Proceedings of the National Academy of Sciences of the United States of America},\n\tauthor = {Stricker, Jesse and Maddox, Paul and Salmon, E D and Erickson, Harold P},\n\tmonth = mar,\n\tyear = {2002},\n\tpmid = {11854462},\n\tkeywords = {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},\n\tpages = {3171--3175}\n}\n\n","author_short":["Stricker, J.","Maddox, P.","Salmon, E D","Erickson, H. P"],"key":"stricker_rapid_2002","id":"stricker_rapid_2002","bibbaseid":"stricker-maddox-salmon-erickson-rapidassemblydynamicsoftheescherichiacoliftszringdemonstratedbyfluorescencerecoveryafterphotobleaching-2002","role":"author","urls":{"Paper":"http://www.ncbi.nlm.nih.gov/pubmed/11854462"},"keyword":["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"],"downloads":0},"search_terms":["rapid","assembly","dynamics","escherichia","coli","ftsz","ring","demonstrated","fluorescence","recovery","photobleaching","stricker","maddox","salmon","erickson"],"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"],"authorIDs":[],"dataSources":["QQyXj7M8pdnbq89aP"]}