Journal of Advances in Molecular Biology

Download PDF (322.8 KB) PP. 31 - 38 Pub. Date: September 30, 2020

DOI: 10.22606/jamb.2020.43001

• Zehui Zhang^*
  School of life science, Tsinghua University, Beijing, China
• Rui Zhang
  School of Medicine, The Capital Medial University, Beijing, China

In many bacteria, cell division is initiated by a tubulin-like protein FtsZ, which forms a ring structure known as the Z-ring at midcell. FtsA and SepF are important membrane anchor of Z-ring, which exists widely in bacteria species and binds to the membrane by a C-terminal amphipathic α-helix in a membrane potential-dependent manner. It reported that amphipathic α-helix binds to the leading edge of developing septum with an intrinsic preference. These discoveries led to a hypothesis, proteins of amphipathic helix might not only function as membrane anchor of FtsZ, but also participating the regulation of septum synthesis. Several variants were made by genetic techniques, and cell length measurements were performed by fluorescence microscopy and ImageJ. All helix variants were found viable, the amphipathic α-helix does affect the cell division but does not affect the functionality.

Bacillus Subtilis, microbial proteins

[1] 1. Nakano, M. M., & Zuber, P. (1998). Anaerobic growth of a “strict aerobe” (Bacillus subtilis). Annual Review of Microbiology, 52, 165–90.

[2] 2. Madigan, M. T. (2005). Brock Biology of Microorganisms, 11th edn. International Microbiology, 8, 149–152.

[3] 3. Rampelotto, P. H. (2010). Resistance of microorganisms to extreme environmental conditions and its contribution to astrobiology. Sustainability, 2(6), 1602–1623.

[4] 4. Moriya, S., Kawai, Y., Kaji, S., Smith, A., Harry, E. J., & Errington, J. (2009). Effects of oriC relocation on control of replication initiation in Bacillus subtilis. Microbiology, 155(9), 3070–3082.

[5] 5. Nanninga, N., & Koppes, L. J. H. (1979). The Cell Cycle of Bacillus subtilis as Studied by Electron Microscopy. Archives of Microbiology, 181, 173–181.

[6] 6. Erickson, H. P. (2001). The FtsZ protofilament and attachment of ZipA - Structural constraints on the FtsZ power stroke. Current Opinion in Cell Biology.

[7] 7. Land, A. D., Luo, Q., & Levin, P. A. (2014). Functional domain analysis of the cell division inhibitor EzrA. PLoS One, 9(7), e102616.

[8] 8. Pichoff, S., & Lutkenhaus, J. (2005). Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Molecular Microbiology, 55(6), 1722–1734.

[9] 9. van den Ent, F., & L?we, J. (2000). Crystal structure of the cell division protein FtsA from Thermotoga maritima. The EMBO Journal, 19(20), 5300–7.

[10] 10. Szwedziak, P., Wang, Q., Freund, S. M., & L?we, J. (2012). {FtsA} forms actin-like protofilaments. {EMBO} J., 31(10), 2249–2260.

[11] 11. Singh, P., Makde, R. D., Ghosh, S., Asthana, J., Kumar, V., & Panda, D. (2013). Assembly of Bacillus subtilis FtsA: Effects of pH, ionic strength and nucleotides on FtsA assembly. International Journal of Biological Macromolecules, 52(1), 170–176.

[12] 12. Ma, X., & Margolin, W. (1999). Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ. Journal of Bacteriology, 181(24), 7531–7544. Retrieved from

[13] 13. Hamoen, L. W., Meile, J. C., De Jong, W., Noirot, P., & Errington, J. (2006). SepF, a novel FtsZ-interacting protein required for a late step in cell division. Molecular Microbiology, 59(3), 989–999.

[14] 14. Duman, R., Ishikawa, S., Celik, I., Strahl, H., Ogasawara, N., Troc, P., … Hamoen, L. W. (2013b). Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring. Proceedings of the National Academy of Sciences of the United States of America, 110(48), E4601-10.

[15] 15. Gundogdu, M. E., Kawai, Y., Pavlendova, N., Ogasawara, N., Errington, J., Scheffers, D. J., & Hamoen, L. W. (2011). Large ring polymers align FtsZ polymers for normal septum formation. EMBO J, 30(3), 617–626.

[16] 16. Zimmerberg, J., & Kozlov, M. M. (2006). How proteins produce cellular membrane curvature. Nature Reviews Molecular Cell Biology, 7(1), 9–19.

[17] 17. Gibson, D. G., Young, L., Chuang, R.-Y., Venter, J. C., Hutchison, C. A., & Smith, H. O. (2009). Enzymatic assembly of DNA molecules up to several hundred kilobases. Nature Methods, 6(5), 343–345.

[18] 18. Gamba, P., Veening, J. W., Saunders, N. J., Hamoen, L. W., & Daniel, R. A. (2009). Two-step assembly dynamics of the Bacillus subtilis divisome. Journal of Bacteriology, 191(13), 4186–4194.

[19] 19. Strahl, H., & Hamoen, L. W. (2010). Membrane potential is important for bacterial cell division. Proceedings of the National Academy of Sciences of the United States of America, 107(27), 12281–6.