Strong FtsZ is with the force: mechanisms to constrict bacteria.
FtsZ, the best-known prokaryotic division protein, assembles at midcell with other proteins forming a ring during septation. Widely conserved in bacteria, FtsZ represents the ancestor of tubulin. In the presence of GTP it forms polymers able to associate into multi-stranded flexible structures. FtsZ research is aimed at determining the role of the Z-ring in division, describing the polymerization and potential force-generating mechanisms and evaluating the roles of nucleotide exchange and hydrolysis. Systems to reconstruct the FtsZ ring in vitro have been described and some of its mechanical properties have been reproduced using in silico modeling. We discuss current research in FtsZ, some of the controversies, and finally propose further research needed to complete a model of FtsZ action that reconciles its in vitro properties with its role in division.
Mingorance
Jesús
J
Unidad de Investigación y Servicio de Microbiología, Hospital Universitario La Paz (IdiPAZ), Paseo de La Castellana, 261, 28046 Madrid, Spain. jmingorancec.hulp@salud.madrid.org
Rivas
Germán
G
Vélez
Marisela
M
Gómez-Puertas
Paulino
P
Vicente
Miguel
M
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002455:Cell Division / Q000502:physiology*; D017358:Cell Wall Skeleton / Q000737:chemistry / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D020558:GTP Phosphohydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D001426:Bacterial Proteins; D017358:Cell Wall Skeleton; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D006160:Guanosine Triphosphate; D020558:GTP Phosphohydrolases