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SepF Increases the Assembly and Bundling of FtsZ Polymers and Stabilizes FtsZ Protofilaments by Binding along Its Length

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Title SepF Increases the Assembly and Bundling of FtsZ Polymers and Stabilizes FtsZ Protofilaments by Binding along Its Length
 
Creator SINGH, JK
MAKDE, RD
KUMAR, V
PANDA, D
 
Subject cell-division protein
bacillus-subtilis
escherichia-coli
interacting protein
bacterial division
gtp hydrolysis
z-ring
membrane
zipa
polymerization
 
Description SepF (Septum Forming) protein has been recently identified through genetic studies, and it has been suggested to be involved in the division of Bacillus subtilis cells. We have purified functional B. subtilis SepF from the inclusion bodies overexpressed in Escherichia coli. Far-UV circular dichroism and fluorescence spectroscopic analysis involving the extrinsic fluorescent probe 1-anilinonaphthalene-8-sulfonic acid suggested that the purified SepF had characteristics of folded proteins. SepF was found to promote the assembly and bundling of FtsZ protofilaments using three complimentary techniques, namely 90 light scattering, sedimentation, and transmission electron microscopy. SepF also decreased the critical concentration of FtsZ assembly, prevented the dilution-induced disassembly of FtsZ protofilaments, and suppressed the GTPase activity of FtsZ. Further, thick bundles of FtsZ protofilaments were observed using fluorescein isothiocyanate-labeled SepF (FITC-SepF). Interestingly, FITC-SepF was found to be uniformly distributed along the length of the FtsZ protofilaments, suggesting that SepF copolymerizes with FtsZ. SepF formed a stable complex with FtsZ, as evident from the gel filtration analysis. Using a C-terminal tail truncated FtsZ (FtsZ Delta 16) and a C-terminal synthetic peptide of B. subtilis FtsZ (366-382); we provided evidence indicating that SepF binds primarily to the C-terminal tail of FtsZ. The present work in concert with the available in vivo data support a model in which SepF plays an important role in regulating the assembly dynamics of the divisome complex; therefore, it may have an important role in bacterial cell division.
 
Publisher AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
 
Date 2011-07-17T05:38:08Z
2011-12-26T12:50:08Z
2011-12-27T05:36:09Z
2011-07-17T05:38:08Z
2011-12-26T12:50:08Z
2011-12-27T05:36:09Z
2008
 
Type Article
 
Identifier JOURNAL OF BIOLOGICAL CHEMISTRY, 283(45), 31116-31124
0021-9258
http://dx.doi.org/10.1074/jbc.M805910200
http://dspace.library.iitb.ac.in/xmlui/handle/10054/4628
http://hdl.handle.net/10054/4628
 
Language en