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Immediate GTP hydrolysis upon FtsZ polymerization
- Source :
- Molecular Microbiology, 43(6), 1517-1521. Wiley
- Publication Year :
- 2002
-
Abstract
- To understand the polymerization dynamics of FtsZ, a bacterial cell division protein similar to tubulin, insight is required into the nature of the nucleotide bound to the polymerized protein. In a previous study, we showed that the FtsZ polymers contain mostly GDP. A recent study challenged this result, suggesting that the polymerized FtsZ is in a GTP-bound state. Here, we show that, when radiolabelled [gamma-32P]-GTP is used to polymerize FtsZ, GTP is hydrolysed instantaneously. The FtsZ polymer contains both GDP and the radiolabelled inorganic phosphate.
- Subjects :
- GTP'
CELL-DIVISION
TUBULIN
macromolecular substances
GTPase
physiological processes
Microbiology
Guanosine Diphosphate
Phosphates
Biopolymers
Bacterial Proteins
Microtubule
Nucleotide
Cytoskeleton
FtsZ
Molecular Biology
GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries)
chemistry.chemical_classification
biology
MICROTUBULE
Hydrolysis
technology, industry, and agriculture
SHEETS
DIVISION PROTEIN FTSZ
Cytoskeletal Proteins
BINDING-PROTEIN
Tubulin
chemistry
Biochemistry
Polymerization
ESCHERICHIA-COLI
biology.protein
ComputingMethodologies_DOCUMENTANDTEXTPROCESSING
bacteria
Chromatography, Thin Layer
Guanosine Triphosphate
biological phenomena, cell phenomena, and immunity
Dimerization
FORM
Subjects
Details
- Language :
- Dutch; Flemish
- ISSN :
- 0950382X
- Volume :
- 43
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Molecular Microbiology
- Accession number :
- edsair.doi.dedup.....f045e4f5c08ffa8c0bae573b7536364b