Immediate GTP hydrolysis upon FtsZ polymerization

Molecular Microbiology

Volumn 43, Issue 6, 2002, Pages 1517-1521

  Scheffers, Dirk Jan ^a,b   Driessen, Arnold J M ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; FTSZ PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; NUCLEOTIDE; PHOSPHATE; PHOSPHORUS 32; POLYMER; TUBULIN;

ARTICLE; BACTERIAL CELL; CELL DIVISION; HYDROLYSIS; ISOTOPE LABELING; PRIORITY JOURNAL; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE;

BACTERIAL PROTEINS; BIOPOLYMERS; CHROMATOGRAPHY, THIN LAYER; CYTOSKELETAL PROTEINS; DIMERIZATION; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; PHOSPHATES;

BACTERIA (MICROORGANISMS);

EID: 0036268368     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2002.02828.x     Document Type: Article

References (27)

1. GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules
2. The essential bacterial cell-division protein FtsZ is a GTPase
3. Microtubule polymerization dynamics
4. Activation of cell division protein FtsZ: Control of switch loop T3 conformation by the nucleotide γ-phosphate
5. Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers
6. Crystal structure of the bacterial cell-division protein FtsZ
7. 2+-induced FtsZ sheets
8. FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritime - Quantitation, GTP hydrolysis, and assembly
9. Themes and variations in prokaryotic cell division
10. Escherichia coli FtsZ polymers contain mostly GTP and have a high nucleotide turnover
11. Dynamic assembly of FtsZ regulated by GTP hydrolysis
12. Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations
13. Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein
14. Assembly of an FtsZ mutant deficient in GTPase activity has implications for FtsZ assembly and the role of the Z ring in cell division
15. Structural insights into microtubule function
16. Tubulin and FtsZ form a distinct family of GTPases
17. High-resolution model of the microtubule
18. Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein
19. Magnesium-induced linear self association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly
20. Direct observation of the enhancement of noncooperative protein self-assembly by macromolecular crowding: Indefinite linear self association of bacterial cell division protein FtsZ
21. Polymerization of FtsZ, a bacterial homolog of tubulin: Is assembly cooperative?
22. The polymerization mechanism of the bacterial cell division protein FtsZ
23. Non-hydrolysable GTP-γ-S stabilizes the FtsZ polymer in a GDP-bound state
24. Substitution of a conserved aspartate allows cation-induced polymerization of FtsZ
25. GTP-hydrolysis of cell division protein FtsZ: Evidence that the active site is formed by the association of monomers
26. Self-activation of guanosine triphosphatase activity by oligomerization of the bacterial cell division protein FtsZ
27. The FtsZ protein of Bacillus subtilis is localized at the division site and has GTPase activity that is dependent upon FtsZ concentration