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Immediate GTP hydrolysis upon FtsZ polymerization
Author(s) -
Scheffers DirkJan,
Driessen Arnold J. M.
Publication year - 2002
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2002.02828.x
Subject(s) - ftsz , gtp' , tubulin , biology , polymerization , cell division , biochemistry , cytoskeleton , guanosine diphosphate , gtpase , guanosine triphosphate , hydrolysis , nucleotide , microbiology and biotechnology , biophysics , microtubule , polymer , cell , chemistry , enzyme , gene , organic chemistry
Summary To understand the polymerization dynamics of FtsZ, a bacterial cell division protein similar to tubulin, insight is required into the nature of the nucleotide bound to the polymerized protein. In a previous study, we showed that the FtsZ polymers contain mostly GDP. A recent study challenged this result, suggesting that the polymerized FtsZ is in a GTP‐bound state. Here, we show that, when radiolabelled [ γ ‐ 32 P]‐GTP is used to polymerize FtsZ, GTP is hydrolysed instantaneously. The FtsZ polymer contains both GDP and the radiolabelled inorganic phosphate.