The FtsZ protofilament and attachment of ZipA - Structural constraints on the FtsZ power stroke

Current Opinion in Cell Biology

Volumn 13, Issue 1, 2001, Pages 55-60

  Erickson, H P ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FTSZ PROTEIN; MEMBRANE PROTEIN; PROTEIN ZIPA; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMNION BAND; CARBOXY TERMINAL SEQUENCE; CELL DIVISION; CELL INTERACTION; CELL MEMBRANE TRANSPORT; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; REVIEW; TEMPERATURE SENSITIVE MUTANT;

BACTERIA (MICROORGANISMS);

EID: 0035146299     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00174-5     Document Type: Review

References (28)

1. Bacterial cell division and the Z ring
2. Bacterial cell division
3. FtsZ, a tubulin homolog, in prokaryote cell division
4. Bacterial cell division
5. Themes and variations in prokaryotic cell division
6. Crystal structure of the bacterial cell-division protein FtsZ
7. Structure of the alphabeta tubulin dimer by electron crystallography
8. Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers
9. Tubulin-like protofilaments in Ca2+-induced FtsZ sheets
10. Straight and curved conformations of FtsZ are regulated by GTP hydrolysis
11. Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to a/β and γ tubulin
12. Bacterial SOS checkpoint protein SulA inhibits polymerization of purified FtsZ cell division protein
13. Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E-coli
14. Recruitment of ZipA to the septal ring of Escherichia coli is dependent on FtsZ and independent of FtsA
15. Recruitment of ZipA to the division site by interaction with FtsZ
16. ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division
17. ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains
18. Temperature shift experiments with ftsZ 84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated
19. Control of ftsZ expression, cell division, and glutamine metabolism in Luria-Bertani medium by the alarmone ppGpp in Escherichia coli
20. The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography
21. Solution structure of ZipA, a crucial component of Escherichia coli cell division
22. Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli ftsZ
23. Analysis of the interaction of FtsZ with itself, GTP, and FtsA
24. A conserved residue at the extreme C-terminus of FtsZ is critical for the FtsA-FtsZ interaction in Staphylococcus aureus
25. Dominant C-terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA
26. Helical tubes of FtsZ from Methanococcus jannaschii
27. Role of the carboxy terminus of Escherichia coli FtsA in self-interaction and cell division
28. Crystal structure of the cell division protein FtsA from Thermotoga maritima