FtsA

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FtsA
FtsA
according to PDB  1e4g

Existing structural data : 1e4g , 1e4f

Mass / length primary structure 45,330 daltons / 420 amino acids
Identifier
External IDs
Enzyme classification
EC, category ,  ATPase
Substrate Adenosine triphosphate
Products Adenosine diphosphate and phosphate

FtsA (from English filamentous temperature sensitive A , filamentous temperature sensitive A ') is a protein of the cytoskeleton of bacteria , with the exception of actinobacteria and cyanobacteria .

properties

Localization of the FtsA on the septum during cell division

FtsA is used in bacteria to stabilize the cell and to move ( cell motility ), it is possibly involved in the initiation of cell division . FtsA is a homolog of actin and a scaffold protein , as are the proteins MreB , ParM and MamK . Like actin, FtsA hydrolyzes adenosine triphosphate to change its conformation and then forms strand-like aggregates ( microfilaments ).

FtsA has a similar structure to PilM , which occurs as type IV ATPase in the pili of bacteria. FtsA binds to FtsZ in the Z-ring and binds it to the cell membrane via an amphiphilic α-helix at the C terminus of the FtsA . Alternatively, the C terminus can also be linked by MinC and ZipA . FtsN is bound at another point on the protein surface. FtsZ, FtsA and ZipA are involved in initiating cell movement. While FTSA in Escherichia coli is essential, its function can in Bacillus subtilis with a deletion by Sepf be partially compensated. The mutant FtsA * works independently of ZipA . Other mutants identified have altered multimerization properties . The functions of the FTSA are different types of bacteria preserved .

Individual evidence

  1. ↑ Geissler B, Shiomi D, Margolin W: The ftsA * gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring . In: Microbiology . 153, No. Pt 3, 2007, pp. 814-823. doi : 10.1099 / mic.0.2006 / 001834-0 . PMID 17322202 .
  2. ^ Van den Ent F, Löwe J: Crystal structure of the cell division protein FtsA from Thermotoga maritima . In: EMBO J . 19, No. 20, 2000, pp. 5300-5307. doi : 10.1093 / emboj / 19.20.5300 . PMID 11032797 .
  3. ↑ a b Szwedziak P, Wang Q, Freund SMV, Löwe J: FtsA forms actin-like protofilaments . In: EMBO J . 31, No. 10, 2012, pp. 2249-2260. doi : 10.1038 / emboj.2012.76 . PMID 22473211 .
  4. ↑ a b c Pichoff S, Shen B, Sullivan B, Lutkenhaus J: 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 . In: Mol Microbiol . 83, No. 6, 2012, pp. 151-167. doi : 10.1111 / j.1365-2958.2011.07923.x . PMID 22111832 .
  5. ↑ Karrupiah F, Derrick JP: Structure of the PilM-PilN inner membrane type IV pilus biogenesis complex from Thermus thermophilus . In: J Biol Chem . 286, No. 27, 2011, pp. 24434-24442. doi : 10.1074 / jbc.M111.243535 . PMID 21596754 .
  6. ↑ Pichoff S, Lutkenhaus J: Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FTSA . In: Mol Microbiol . 55, No. 6, 2005, pp. 1722-1734. doi : 10.1111 / j.1365-2958.2005.04522.x . PMID 15752196 .
  7. ↑ Rico AI, García-Ovalle M, Mingorance J, Vicente M: Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring . In: Mol Microbiol . 53, No. 5, Sep 2004, pp. 1359-1371year = 2004. doi : 10.1111 / j.1365-2958.2004.04245.x . PMID 15387815 .
  8. ↑ Busiek KK, Eraso JM, Wang Y, Margolin W: The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN . In: J Bacteriol . 194, No. 8, 2012, pp. 1989-2000. doi : 10.1128 / JB.06683-11 . PMID 22328664 .
  9. ^ Rico AI, Krupka M, Vicente M: In the beginning, Escherichia coli assembled the proto-ring: an initial phase of division . In: J Biol Chem . 288, No. 29, 2013, pp. 20830-20836. doi : 10.1074 / jbc.R113.479519 . PMID 23740256 .
  10. ↑ Ishikawa S, Kawai Y, Hiramatsu K, Kuwano M, Ogasawara N: A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis . In: Mol Microbiol . 60, No. 1, 2006, pp. 1364-1380. doi : 10.1111 / j.1365-2958.2006.05184.x . PMID 16796675 .
  11. ↑ Geissler B, Elraheb D, Margolin W: A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli . In: Proc Natl Acad Sci USA . 100, No. 7, 2003, pp. 4197-4202. doi : 10.1073 / pnas.0635003100 . PMID 12634424 .
  12. ↑ Osawa M, Erickson HP: Liposome division by a simple bacterial division machinery . In: Proc Natl Acad Sci USA . 110, No. 3, 2013, pp. 11000–11004. doi : 10.1073 / pnas.1222254110 . PMID 25213228 .
  13. ↑ Fujita J, Maeda Y, Nagao C, Tsuchiya Y, Miyazaki Y, Hirose M, Mizohata E, Matsumoto Y, Inoue T, Mizuguchi K, Matsumura H: Crystal structure of FtsA from Staphylococcus aureus . In: FEBS Lett . 588, No. 10, 2014, pp. 1879–1885. doi : 10.1016 / j.febslet.2014.04.008 . PMID 24746687 .