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Biology

FtsZ полимеризации Анализы: Простые протоколы и соображения

Published: November 16, 2013 doi: 10.3791/50844

Materials

Name Company Catalog Number Comments
GTP Roche 10106399001 Part 1, 2, 3, 4, 5, 6, 7
Thickwall Polycarbonate Tubes Beckman Coulter 343776 Part 2
Optima MAX-XP Ultracentrifuge Beckman Coulter 393315 Part 2, 3
Polyallomer Tube with Snap-on Cap Beckman Coulter 357448 Part 3
AIDA Bio-package, 1D, 2D, FL Raytest Isotopenmessgeräte GmbH 15000001 Part 4
Luminescence Image Analyzer LAS-4000 Fujifilm Part 4
Thermo Spectronic AMINCO-Bowman Luminescence Spectrometer Spectronic Instruments Part 5
Fluorescence Cell Hellma Analytics 105-250-15-40 Part 5
Square 400 Mesh, Copper, 100/vial Electron Microscopy Sciences G400-Cu Part 6
CM120 Electron Microscope Operating at 120 kV Philips Part 6
96 ml x 0.2 ml Plate BIOplastics B70501 Part 7
Malachite Green Phosphate Assay Kit BioAssay System POMG-25H Part 7
PowerWave HT Microplate Spectrophotometer BioTek Part 7

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References

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  2. Adams, D. W., Errington, J. Bacterial cell division: assembly, maintenance and disassembly of the Z ring. Nat. Rev. Microbiol. 7 (9), 642-653 (2009).
  3. Erickson, H. P., Anderson, D. E., Osawa, M. FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol. Mol. Biol. Rev. 74 (4), 504-528 (2010).
  4. Li, Z., Trimble, M. J., Brun, Y. V., Jensen, G. J. The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J. 26 (22), 4694-4708 (2007).
  5. Król, E., van Kessel, S. P., van Bezouwen, L. S., Kumar, N., Boekema, E. J., Scheffers, D. J. Bacillus subtilis SepF binds to the C-terminus of FtsZ. PLoS One. 7 (8), e43293 (2012).
  6. Singh, J. K., Makde, R. D., Kumar, V., Panda, D. SepF increases the assembly and bundling of FtsZ polymers and stabilizes FtsZ protofilaments by binding along its length. J. Biol. Chem. 283 (45), 31116-31124 (2008).
  7. Gündoğdu, M. E., Kawai, Y., et al. Large ring polymers align FtsZ polymers for normal septum formation. EMBO J. 30 (3), 617-626 (2011).
  8. Pacheco-Gomez, R., Roper, D. I., Dafforn, T. R., Rodger, A. The pH dependence of polymerization and bundling by the essential bacterial cytoskeletal protein FtsZ. PLoS One. 6 (6), e19369 (2011).
  9. Mendieta, J., Rico, A. I., Lopez-Vinas, E., Vicente, M., Mingorance, J., Gomez-Puertas, P. Structural and functional model for ionic (K(+)/Na(+)) and pH dependence of GTPase activity and polymerization of FtsZ, the prokaryotic ortholog of tubulin. J. Mol. Biol. 390 (1), 17-25 (2009).
  10. Tadros, M., Gonzalez, J. M., Rivas, G., Vicente, M., Mingorance, J. Activation of the Escherichia coli cell division protein FtsZ by a low-affinity interaction with monovalent cations. FEBS Lett. 580 (20), 4941-4946 (2006).
  11. Scheffers, D. J. The effect of MinC on FtsZ polymerization is pH dependent and can be counteracted by ZapA. FEBS Lett. 582 (17), 2601-2608 (2008).
  12. Mukherjee, A., Lutkenhaus, J. Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations. J. Bacteriol. 181 (3), 823-832 (1999).
  13. Chen, Y., Erickson, H. P. Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer. J. Biol. Chem. 280 (23), 22549-22554 (2005).
  14. Hou, S., Wieczorek, S. A., et al. Characterization of Caulobacter crescentus FtsZ protein using dynamic light scattering. J. Biol. Chem. 287 (28), 23878-23886 (2012).
  15. Mukherjee, A., Lutkenhaus, J. Dynamic assembly of FtsZ regulated by GTP hydrolysis. EMBO J. 17 (2), 462-469 (1998).
  16. Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., Candia, O. A. An improved assay for nanomole amounts of inorganic phosphate. Anal. Biochem. 100 (1), 95-97 (1979).
  17. Ray, S., Kumar, A., Panda, D. GTP regulates the interaction between MciZ and FtsZ: a possible role of MciZ in bacterial cell division. Biochemistry. 52 (2), 392-401 (2013).
  18. Rivas, G., Lopez, A., et al. Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly. J. Biol. Chem. 275 (16), 11740-11749 (2000).
  19. Oliva, M. A., Cordell, S. C., Lowe, J. Structural insights into FtsZ protofilament formation. Nat. Struct. Mol. Biol. 11 (12), 1243-1250 (2004).
  20. Lowe, J., Amos, L. A. Crystal structure of the bacterial cell-division protein FtsZ. Nature. 391 (6663), 203-206 (1998).
  21. Cordell, S. C., Robinson, E. J., Lowe, J. Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ. Proc. Natl. Acad. Sci. U.S.A. 100 (13), 7889-7894 (2003).
  22. Chen, Y., Anderson, D. E., Rajagopalan, M., Erickson, H. P. Assembly dynamics of Mycobacterium tuberculosis FtsZ. J. Biol. Chem. 282 (38), 27736-27743 (2007).
  23. White, E. L., Ross, L. J., Reynolds, R. C., Seitz, L. E., Moore, G. D., Borhani, D. W. Slow polymerization of Mycobacterium tuberculosis FtsZ. J. Bacteriol. 182 (14), 4028-4034 (2000).
  24. Oliva, M. A., Trambaiolo, D., Lowe, J. Structural insights into the conformational variability of FtsZ. J. Mol. Biol. 373 (5), 1229-1242 (2007).
  25. Thanbichler, M., Shapiro, L. M. ipZ. a spatial regulator coordinating chromosome segregation with cell division in Caulobacter. Cell. 126 (1), 147-162 (2006).
  26. Buske, P. J., Levin, P. A. Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins. J. Biol. Chem. 287 (14), 10945-10957 (2012).
  27. Mukherjee, A., Lutkenhaus, J. Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations. J. Bacteriol. 181 (3), 823-832 (1999).
FtsZ полимеризации Анализы: Простые протоколы и соображения
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Król, E., Scheffers, D. J. FtsZ More

Król, E., Scheffers, D. J. FtsZ Polymerization Assays: Simple Protocols and Considerations. J. Vis. Exp. (81), e50844, doi:10.3791/50844 (2013).

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