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Article: Probing FtsZ and Tubulin with C8-Substituted GTP Analogs Reveals Differences in Their Nucleotide Binding Sites

TitleProbing FtsZ and Tubulin with C8-Substituted GTP Analogs Reveals Differences in Their Nucleotide Binding Sites
Authors
KeywordsCHEMBIO
CELLBIO
Issue Date2008
Citation
Chemistry and Biology, 2008, v. 15, n. 2, p. 189-199 How to Cite?
AbstractThe cytoskeletal proteins, FtsZ and tubulin, play a pivotal role in prokaryotic cell division and eukaryotic chromosome segregation, respectively. Selective inhibitors of the GTP-dependent polymerization of FtsZ could constitute a new class of antibiotics, while several inhibitors of tubulin are widely used in antiproliferative therapy. In this work, we set out to identify selective inhibitors of FtsZ based on the structure of its natural ligand, GTP. We found that GTP analogs with small hydrophobic substituents at C8 of the nucleobase efficiently inhibit FtsZ polymerization, whereas they have an opposite effect on the polymerization of tubulin. The inhibitory activity of the GTP analogs on FtsZ polymerization allowed us to crystallize FtsZ in complex with C8-morpholino-GTP, revealing the binding mode of a GTP derivative containing a nonmodified triphosphate chain. © 2008 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/219561
ISSN
2015 Impact Factor: 5.774
2015 SCImago Journal Rankings: 3.282

 

DC FieldValueLanguage
dc.contributor.authorLäppchen, Tilman-
dc.contributor.authorPinas, Victorine A.-
dc.contributor.authorHartog, Aloysius F.-
dc.contributor.authorKoomen, Gerrit Jan-
dc.contributor.authorSchaffner-Barbero, Claudia-
dc.contributor.authorAndreu, José Manuel-
dc.contributor.authorTrambaiolo, Daniel-
dc.contributor.authorLöwe, Jan-
dc.contributor.authorJuhem, Aurélie-
dc.contributor.authorPopov, Andrei V.-
dc.contributor.authorden Blaauwen, Tanneke-
dc.date.accessioned2015-09-23T02:57:24Z-
dc.date.available2015-09-23T02:57:24Z-
dc.date.issued2008-
dc.identifier.citationChemistry and Biology, 2008, v. 15, n. 2, p. 189-199-
dc.identifier.issn1074-5521-
dc.identifier.urihttp://hdl.handle.net/10722/219561-
dc.description.abstractThe cytoskeletal proteins, FtsZ and tubulin, play a pivotal role in prokaryotic cell division and eukaryotic chromosome segregation, respectively. Selective inhibitors of the GTP-dependent polymerization of FtsZ could constitute a new class of antibiotics, while several inhibitors of tubulin are widely used in antiproliferative therapy. In this work, we set out to identify selective inhibitors of FtsZ based on the structure of its natural ligand, GTP. We found that GTP analogs with small hydrophobic substituents at C8 of the nucleobase efficiently inhibit FtsZ polymerization, whereas they have an opposite effect on the polymerization of tubulin. The inhibitory activity of the GTP analogs on FtsZ polymerization allowed us to crystallize FtsZ in complex with C8-morpholino-GTP, revealing the binding mode of a GTP derivative containing a nonmodified triphosphate chain. © 2008 Elsevier Ltd. All rights reserved.-
dc.languageeng-
dc.relation.ispartofChemistry and Biology-
dc.subjectCHEMBIO-
dc.subjectCELLBIO-
dc.titleProbing FtsZ and Tubulin with C8-Substituted GTP Analogs Reveals Differences in Their Nucleotide Binding Sites-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.chembiol.2007.12.013-
dc.identifier.pmid18291323-
dc.identifier.scopuseid_2-s2.0-39149144502-
dc.identifier.volume15-
dc.identifier.issue2-
dc.identifier.spage189-
dc.identifier.epage199-

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