Open AccessGuanine nucleotide-dependent assembly of FtsZ into filaments
Author(s) -
Amit Mukherjee,
Joe Lutkenhaus
Publication year - 1994
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.176.9.2754-2758.1994
Subject(s) - ftsz , gtpase , gtp' , biology , tubulin , nucleotide , cell division , guanosine triphosphate , guanine , cytoskeleton , microbiology and biotechnology , cytokinesis , biochemistry , gtp binding protein regulators , microtubule , g protein , cell , enzyme , gene , signal transduction
FtsZ is an essential cell division protein that is localized to the leading edge of the bacterial septum in a cytokinetic ring. It contains the tubulin signature motif and is a GTP binding protein with a GTPase activity. Further comparison of FtsZ with eukaryotic tubulins revealed some additional sequence similarities, perhaps indicating a similar GTP binding site. Examination of FtsZ incubated in vitro by electron microscopy revealed a guanine nucleotide-dependent assembly into protein filaments, supporting the hypothesis that the FtsZ ring is formed through self-assembly. FtsZ3, which is unable to bind GTP, does not polymerize, whereas FtsZ2, which binds GTP but is deficient in GTP hydrolysis, is capable of polymerization.