Substitution of a conserved aspartate allows cation-induced polymerization of FtsZ
| Autor: | Janny G. de Wit, Dirk-Jan Scheffers, Arnold J. M. Driessen, Tanneke den Blaauwen |
|---|---|
| Přispěvatelé: | Groningen Biomolecular Sciences and Biotechnology, Moleculaire Microbiologie, Molecular Cytology (SILS, FNWI) |
| Jazyk: | Dutch; Flemish |
| Rok vydání: | 2001 |
| Předmět: |
GTP'
Cell division Cations Divalent Polymers Mutant Biophysics macromolecular substances medicine.disease_cause physiological processes Biochemistry FtsZ Divalent Polymerization Residue (chemistry) Bacterial Proteins Structural Biology Tubulin Genetics medicine Nucleotide GeneralLiterature_REFERENCE(e.g. dictionaries encyclopedias glossaries) Molecular Biology Escherichia coli chemistry.chemical_classification Aspartic Acid Cation biology Chemistry Cell Biology Cytoskeletal Proteins Amino Acid Substitution Mutagenesis Site-Directed ComputingMethodologies_DOCUMENTANDTEXTPROCESSING biology.protein bacteria Guanosine Triphosphate biological phenomena cell phenomena and immunity |
| Zdroj: | FEBS Letters, 494(1-2), 34-37. Wiley FEBS Letters, 494, 34-37. Wiley-Blackwell |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/S0014-5793(01)02310-9 |
| Popis: | The prokaryotic tubulin homologue FtsZ polymerizes in vitro in a nucleotide dependent fashion. Here we report that replacement of the strictly conserved Asp212 residue of Escherichia coli FtsZ by a Cys or Asn, but not by a Glu residue results in FtsZ that polymerizes with divalent cations in the absence of added GTP. FtsZ D212C and D212N mutants co-purify with GTP as bound nucleotide, providing an explanation for the unusual phenotype. We conclude that D212 plays a critical role in the coordination of a metal ion and the nucleotide at the interface of two FtsZ monomers. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text