FtsA

Cell division protein FtsA

E. coli cells producing FtsA-GFP, which localizes to the cell division site.
Identifiers
Organism Escherichia coli (strain K12)
Symbol FtsA
Entrez 944778
RefSeq (Prot) NP_414636.1
UniProt P0ABH0
Other data
Chromosome Genome: 0.1 - 0.11 Mb

FtsA is a bacterial protein that is related to actin by overall structural similarity and in its ATP binding pocket.[1][2][3]

Along with other bacterial actin homologs such as MreB, ParM, and MamK, these proteins suggest that eukaryotic actin has a common ancestry. Like the other bacterial actins, FtsA binds ATP and can form actin-like filaments.[4] The FtsA-FtsA interface has been defined by structural as well as genetic analysis.[5] Although present in many diverse Gram-positive and Gram-negative species, FtsA is absent in actinobacteria and cyanobacteria. FtsA also is structurally similar to PilM, a type IV pilus ATPase.[6]

Function

FtsA is required for proper cytokinesis in bacteria such as Escherichia coli, Caulobacter crescentus, and Bacillus subtilis. Originally isolated in a screen for E. coli cells that could not divide at 42˚C but could at 30˚C, FtsA stands for “filamentous temperature sensitive A”. Many thermosensitive alleles of E. coli ftsA exist, and all map in or near the ATP binding pocket. Suppressors that restore normal function map either to the binding pocket or to the FtsA-FtsA interface.[7]

FtsA localizes to the cytokinetic ring formed by FtsZ (Z ring). One of FtsA's functions in cytokinesis is to tether FtsZ polymers to the cytoplasmic membrane via a conserved C-terminal amphipathic helix.[8] Another essential division protein, ZipA, also tethers the Z ring to the membrane and exhibits overlapping function with FtsA. FtsZ, FtsA and ZipA together are called the proto-ring because they are involved in a specific initial phase of cytokinesis.[9] Removal of this helix results in the formation of very long and stable polymer bundles of FtsA in the cell that do not function in cytokinesis.[5] Another subdomain of FtsA (2B) is required for interactions with FtsZ, via the conserved C-terminus of FtsZ [4] Other FtsZ regulators including MinC and ZipA bind to the same C terminus of FtsZ. Finally, subdomain 1C, which is in a unique position relative to MreB and actin, is required for FtsA to recruit downstream cell division proteins such as FtsN.[10][11]

Although FtsA is essential for viability in E. coli, it can be deleted in B. subtilis. B. subtilis cells lacking FtsA divide poorly, but still survive. Another FtsZ-interacting protein, SepF (originally named YlmF), is able to replace FtsA in B. subtilis, suggesting that SepF and FtsA have overlapping functions.[12]

An allele of FtsA called FtsA* (R286W) is able to bypass the normal requirement for the ZipA in E. coli cytokinesis.[13] FtsA* also causes cells to divide at a shorter cell length than normal, suggesting that FtsA may normally receive signals from the septum synthesis machinery to regulate when cytokinesis can proceed.[14] Other FtsA*-like alleles have been found, and they mostly decrease FtsA-FtsA interactions.[5] Oligomeric state of FtsA is likely important for regulating its activity and its ability to bind ATP.[7] Other cell division proteins of E. coli, including FtsN and the ABC transporter homologs FtsEX, seem to regulate septum constriction by signaling through FtsA,[15][16] and the FtsQLB subcomplex is also involved in promoting FtsN-mediated septal constriction.[17][18]

FtsA binds directly to the conserved C-terminal domain of FtsZ.[4] This FtsA-FtsZ interaction is likely involved in regulating FtsZ polymer dynamics. In vitro, E. coli FtsA disassembles FtsZ polymers in the presence of ATP, both in solution, as FtsA* [19] and on supported lipid bilayers.[20] FtsA from Streptococcus pneumoniae forms helical filaments in the presence of ATP,[21] but no interactions with FtsZ have been reported yet. FtsA from Staphylococcus aureus forms actin-like filaments similar to those of FtsA from Thermotoga maritima.[22] In addition, S. aureus FtsA enhances the GTPase activity of FtsZ. In a liposome system, FtsA* stimulates FtsZ to form rings that can divide liposomes, mimicking cytokinesis in vitro.[23]

References

  1. ↑ van den Ent F, Löwe J (Oct 2000). "Crystal structure of the cell division protein FtsA from Thermotoga maritima". The EMBO Journal. 19 (20): 5300–7. doi:10.1093/emboj/19.20.5300. PMID 11032797.
  2. ↑ Gunning PW, Ghoshdastider U, Whitaker S, Popp D, Robinson RC (Jun 2015). "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science. 128 (11): 2009–19. doi:10.1242/jcs.165563. PMID 25788699.
  3. ↑ Ghoshdastider U, Jiang S, Popp D, Robinson RC (Jul 2015). "In search of the primordial actin filament". Proceedings of the National Academy of Sciences of the United States of America. 112 (30): 9150–1. doi:10.1073/pnas.1511568112. PMID 26178194.
  4. 1 2 3 Szwedziak P, Wang Q, Freund SM, Löwe J (May 2012). "FtsA forms actin-like protofilaments". The EMBO Journal. 31 (10): 2249–60. doi:10.1038/emboj.2012.76. PMID 22473211.
  5. 1 2 3 Pichoff S, Shen B, Sullivan B, Lutkenhaus J (Jan 2012). "FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins". Molecular Microbiology. 83 (1): 151–67. doi:10.1111/j.1365-2958.2011.07923.x. PMID 22111832.
  6. ↑ Karuppiah V, Derrick JP (Jul 2011). "Structure of the PilM-PilN inner membrane type IV pilus biogenesis complex from Thermus thermophilus". The Journal of Biological Chemistry. 286 (27): 24434–42. doi:10.1074/jbc.M111.243535. PMID 21596754.
  7. 1 2 Herricks JR, Nguyen D, Margolin W (Nov 2014). "A thermosensitive defect in the ATP binding pocket of FtsA can be suppressed by allosteric changes in the dimer interface". Molecular Microbiology. 94 (3): 713–27. doi:10.1111/mmi.12790. PMID 25213228.
  8. ↑ Pichoff S, Lutkenhaus J (Mar 2005). "Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA". Molecular Microbiology. 55 (6): 1722–34. doi:10.1111/j.1365-2958.2005.04522.x. PMID 15752196.
  9. ↑ Rico AI, Krupka M, Vicente M (Jul 2013). "In the beginning, Escherichia coli assembled the proto-ring: an initial phase of division". The Journal of Biological Chemistry. 288 (29): 20830–6. doi:10.1074/jbc.R113.479519. PMID 23740256.
  10. ↑ Rico AI, García-Ovalle M, Mingorance J, Vicente M (Sep 2004). "Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring". Molecular Microbiology. 53 (5): 1359–71. doi:10.1111/j.1365-2958.2004.04245.x. PMID 15387815.
  11. ↑ Busiek KK, Eraso JM, Wang Y, Margolin W (Apr 2012). "The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN". Journal of Bacteriology. 194 (8): 1989–2000. doi:10.1128/JB.06683-11. PMID 22328664.
  12. ↑ Ishikawa S, Kawai Y, Hiramatsu K, Kuwano M, Ogasawara N (Jun 2006). "A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis". Molecular Microbiology. 60 (6): 1364–80. doi:10.1111/j.1365-2958.2006.05184.x. PMID 16796675.
  13. ↑ Geissler B, Elraheb D, Margolin W (Apr 2003). "A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli". Proceedings of the National Academy of Sciences of the United States of America. 100 (7): 4197–202. doi:10.1073/pnas.0635003100. PMID 12634424.
  14. ↑ Geissler B, Shiomi D, Margolin W (Mar 2007). "The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring". Microbiology. 153 (Pt 3): 814–25. doi:10.1099/mic.0.2006/001834-0. PMID 17322202.
  15. ↑ Du S, Pichoff S, Lutkenhaus J (Aug 2016). "FtsEX acts on FtsA to regulate divisome assembly and activity". Proc Natl Acad Sci USA. 113 (34): 5052–5061. doi:10.1073/pnas.1606656113. PMID 27503875.
  16. ↑ Pichoff S, Du S, Lutkenhaus J (Mar 2015). "The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring". Molecular Microbiology. 95 (6): 971–987. doi:10.1111/mmi.12907. PMID 25496259.
  17. ↑ Tsang MJ, Bernhardt TG (Mar 2015). "A role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates division". Molecular Microbiology. 95 (6): 924–944. doi:10.1111/mmi.12905. PMID 25496050.
  18. ↑ Liu B, Persons L, Lee L, de Boer P (Mar 2015). "Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli". Molecular Microbiology. 95 (6): 945–970. doi:10.1111/mmi.12906. PMID 25496160.
  19. ↑ Beuria TK, Mullapudi S, Mileykovskaya E, Sadasivam M, Dowhan W, Margolin W (May 2009). "Adenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actin-like FtsA". The Journal of Biological Chemistry. 284 (21): 14079–86. doi:10.1074/jbc.M808872200. PMID 19297332.
  20. ↑ Loose M, Mitchison TJ (Jan 2014). "The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns". Nature Cell Biology. 16 (1): 38–46. doi:10.1038/ncb2885. PMID 24316672.
  21. ↑ Lara B, Rico AI, Petruzzelli S, Santona A, Dumas J, Biton J, Vicente M, Mingorance J, Massidda O (2005). "Cell division in cocci: localization and properties of the Streptococcus pneumoniae FtsA protein". Molecular Microbiology. 55 (3): 699–711. doi:10.1111/j.1365-2958.2004.04432.x. PMID 15660997.
  22. ↑ Fujita J, Maeda Y, Nagao C, Tsuchiya Y, Miyazaki Y, Hirose M, Mizohata E, Matsumoto Y, Inoue T, Mizuguchi K, Matsumura H (May 2014). "Crystal structure of FtsA from Staphylococcus aureus". FEBS Letters. 588 (10): 1879–85. doi:10.1016/j.febslet.2014.04.008. PMID 24746687.
  23. ↑ Osawa M, Erickson HP (2013). "Liposome division by a simple bacterial division machinery". Proceedings of the National Academy of Sciences of the United States of America. 110 (27): 11000–4. doi:10.1073/pnas.1222254110. PMC 3703997Freely accessible. PMID 23776220.
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