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The polymerization mechanism of the bacterial cell division protein FtsZ
Author(s) -
Scheffers Dirk-Jan,
Driessen Arnold J.M.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02855-1
Subject(s) - ftsz , tubulin , cell division , polymerization , archaea , microbiology and biotechnology , nucleotide , bacterial cell structure , biochemistry , chemistry , biology , bacteria , biophysics , cell , microtubule , polymer , genetics , gene , organic chemistry
Bacteria and archaea usually divide symmetrically by formation of a septum in the middle of the cell. A key event in cell division is the assembly of the FtsZ ring. FtsZ is the prokaryotic homolog of tubulin and forms polymers in the presence of guanine nucleotides. Here, we specifically address the polymerization of FtsZ and the role of nucleotide hydrolysis in polymer formation and stabilization. Recent structural and biochemical results are discussed and a model for FtsZ polymerization, similar to that for tubulin, is presented.