The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Straight and Curved Conformations of FtsZ Are Regulated by GTP Hydrolysis
Open accessAbstract
FtsZ assembles in vitro into protofilaments that can adopt two conformations—the straight conformation, which can assemble further into two-dimensional protofilament sheets, and the curved conformation, which forms minirings about 23 nm in diameter. Here, we describe the structure of FtsZ tubes, which are a variation of the curved conformation. In the tube the curved protofilament forms a shallow helix with a diameter of 23 nm and a pitch of 18 or 24°. We suggest that this shallow helix is the relaxed structure of the curved protofilament in solution. We provide evidence that GTP favors the straight conformation while GDP favors the curved conformation. In particular, exclusively straight protofilaments and protofilament sheets are assembled in GMPCPP, a nonhydrolyzable GTP analog, or in GTP following chelation of Mg, which blocks GTP hydrolysis. Assembly in GDP produces exclusively tubes. The transition from straight protofilaments to the curved conformation may provide a mechanism whereby the energy of GTP hydrolysis is used to generate force for the constriction of the FtsZ ring in cell division.
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Citations
Cites
The essential bacterial cell-division protein FtsZ is a GTPase
de Boer, P., Crossley, R., & Rothfield, L. (1992) · Nature · doi:10.1038/359254a0 · Cited by 559
BACTERIAL CELL DIVISION AND THE Z RING
Lutkenhaus, J., & Addinall, S. G. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.93 · Cited by 465
Erickson, H. P., Taylor, D. W., Taylor, K. A., & Bramhill, D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.519 · Cited by 459
Self-citationMa, X., Ehrhardt, D. W., & Margolin, W. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.23.12998 · Cited by 444
Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein
RayChaudhuri, D., & Park, J. T. (1992) · Nature · doi:10.1038/359251a0 · Cited by 426
Hyman, A. A., Salser, S., Drechsel, D. N., Unwin, N., & Mitchison, T. J. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.10.1155 · Cited by 398
Guanine nucleotide-dependent assembly of FtsZ into filaments
Mukherjee, A., & Lutkenhaus, J. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.9.2754-2758.1994 · Cited by 379
Dynamic assembly of FtsZ regulated by GTP hydrolysis
Mukherjee, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.2.462 · Cited by 363
Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein.
Mukherjee, A., Dai, K., & Lutkenhaus, J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.3.1053 · Cited by 312
FtsZ, a prokaryotic homolog of tubulin?
Erickson, H. P. (1995) · Cell · doi:10.1016/0092-8674(95)90486-7 · Cited by 300
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Cited by
FtsZ and the division of prokaryotic cells and organelles
Margolin, W. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1745 · Cited by 631
Yang, X., Lyu, Z., Miguel, A., McQuillen, R., Huang, K. C., & Xiao, J. (2017) · Science · doi:10.1126/science.aak9995 · Cited by 482
The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns
Loose, M., & Mitchison, T. J. (2014) · Nature Cell Biology · doi:10.1038/ncb2885 · Cited by 378
Assembly Dynamics of the Bacterial Cell Division Protein FtsZ: Poised at the Edge of Stability
Romberg, L., & Levin, P. A. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.012903.074300 · Cited by 260
Bacterial cytokinesis: From Z ring to divisome
Lutkenhaus, J., Pichoff, S., & Du, S. (2012) · Cytoskeleton · doi:10.1002/cm.21054 · Cited by 260
Metadata
- Authors
- Lu, C., Reedy, M., & Erickson, H. P.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2000-01
- Volume
- 182
- Issue
- 1
- Pages
- 164-170
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- OpenAlex
- W2105986839
- Cited by
- 300
- References
- 27
- FWCI
- 5.66
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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