scholarly journals Bacterial SOS Checkpoint Protein SulA Inhibits Polymerization of Purified FtsZ Cell Division Protein

1998 ◽  
Vol 180 (15) ◽  
pp. 3946-3953 ◽  
Author(s):  
Dorina Trusca ◽  
Solomon Scott ◽  
Chris Thompson ◽  
David Bramhill
Keyword(s):  
Escherichia Coli ◽  
Dna Damage ◽  
Control System ◽  
Cell Division ◽  
Gtpase Activity ◽  
Checkpoint Control ◽  
Checkpoint Protein ◽  
Point Mutant ◽  
Reversible Inhibition ◽  
Cell Division Protein

ABSTRACT Cell division of Escherichia coli is inhibited when the SulA protein is induced in response to DNA damage as part of the SOS checkpoint control system. The SulA protein interacts with the tubulin-like FtsZ division protein. We investigated the effects of purified SulA upon FtsZ. SulA protein inhibits the polymerization and the GTPase activity of FtsZ, while point mutant SulA proteins show little effect on either of these FtsZ activities. SulA did not inhibit the polymerization of purified FtsZ2 mutant protein, which was originally isolated as insensitive to SulA. These studies define polymerization assays for FtsZ which respond to an authentic cellular regulator. The observations presented here support the notion that polymerization of FtsZ is central to its cellular role and that direct, reversible inhibition of FtsZ polymerization by SulA may account for division inhibition.

scholarly journals Contribution of the FtsQ Transmembrane Segment to Localization to the Cell Division Site

2007 ◽  
Vol 189 (20) ◽  
pp. 7273-7280 ◽  
Author(s):  
Dirk-Jan Scheffers ◽  
Carine Robichon ◽  
Gert Jan Haan ◽  
Tanneke den Blaauwen ◽  
Gregory Koningstein ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Membrane Protein ◽  
Cytoplasmic Membrane ◽  
Central Component ◽  
Transmembrane Segment ◽  
Division Site ◽  
Periplasmic Domain ◽  
Cell Division Protein

ABSTRACT The Escherichia coli cell division protein FtsQ is a central component of the divisome. FtsQ is a bitopic membrane protein with a large C-terminal periplasmic domain. In this work we investigated the role of the transmembrane segment (TMS) that anchors FtsQ in the cytoplasmic membrane. A set of TMS mutants was made and analyzed for the ability to complement an ftsQ mutant. Study of the various steps involved in FtsQ biogenesis revealed that one mutant (L29/32R;V38P) failed to functionally insert into the membrane, whereas another mutant (L29/32R) was correctly assembled and interacted with FtsB and FtsL but failed to localize efficiently to the cell division site. Our results indicate that the FtsQ TMS plays a role in FtsQ localization to the division site.

scholarly journals Slow Polymerization of Mycobacterium tuberculosis FtsZ

2000 ◽  
Vol 182 (14) ◽  
pp. 4028-4034 ◽  
Author(s):  
E. Lucile White ◽  
Larry J. Ross ◽  
Robert C. Reynolds ◽  
Lainne E. Seitz ◽  
Georgia D. Moore ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Mycobacterium Tuberculosis ◽  
Tubulin Polymerization ◽  
Gtpase Activity ◽  
Gtp Hydrolysis ◽  
Minimum Concentration ◽  
E Coli ◽  
Cell Division Protein ◽  
Mycobacterial Protein

ABSTRACT The essential cell division protein, FtsZ, from Mycobacterium tuberculosis has been expressed in Escherichia coliand purified. The recombinant protein has GTPase activity typical of tubulin and other FtsZs. FtsZ polymerization was studied using 90° light scattering. The mycobacterial protein reaches maximum polymerization much more slowly (∼10 min) than E. coliFtsZ. Depolymerization also occurs slowly, taking 1 h or longer under most conditions. Polymerization requires both Mg2+and GTP. The minimum concentration of FtsZ needed for polymerization is 3 μM. Electron microscopy shows that polymerized M. tuberculosis FtsZ consists of strands that associate to form ordered aggregates of parallel protofilaments. Ethyl 6-amino-2,3-dihydro-4-phenyl-1H-pyrido[4,3-b][1,4]diazepin-8-ylcarbamate (SRI 7614), an inhibitor of tubulin polymerization synthesized at Southern Research Institute, inhibits M. tuberculosis FtsZ polymerization, inhibits GTP hydrolysis, and reduces the number and sizes of FtsZ polymers.

scholarly journals The Cell Division Protein FtsZ fromStreptococcus pneumoniaeExhibits a GTPase Activity Delay

2015 ◽  
Vol 290 (41) ◽  
pp. 25081-25089 ◽  
Author(s):  
Estefanía Salvarelli ◽  
Marcin Krupka ◽  
Germán Rivas ◽  
Jesus Mingorance ◽  
Paulino Gómez-Puertas ◽  
...  
Keyword(s):  
Cell Division ◽  
Gtpase Activity ◽  
Cell Division Protein

scholarly journals FtsI and FtsW Are Localized to the Septum inEscherichia coli

1998 ◽  
Vol 180 (11) ◽  
pp. 2810-2816 ◽  
Author(s):  
Lilin Wang ◽  
Medhat K. Khattar ◽  
W. D. Donachie ◽  
Joe Lutkenhaus
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Immunofluorescence Microscopy ◽  
Binding Protein ◽  
Specific Inhibitor ◽  
Inescherichia Coli ◽  
Penicillin Binding Protein ◽  
Cell Division Protein

ABSTRACT The localization of FtsI (PBP3), a penicillin-binding protein specifically required for cell division in Escherichia coli, was investigated by immunofluorescence microscopy and found to localize to the septum. The localization of FtsI was not observed inftsZ or ftsA mutants, indicating that it was dependent on the prior localization of these proteins. Addition of furazlocillin, a specific inhibitor of FtsI, prevented localization of FtsI even though FtsZ and FtsA localization occurred. Interestingly, the localization of FtsN was also prevented by furazlocillin. FtsZ displayed limited localization in furazlocillin-treated cells, whereas it was efficiently localized in FtsI-depleted cells. FtsW, another essential cell division protein, was also localized to the septum.

scholarly journals Phenylpropanoids inhibit protofilament formation of Escherichia coli cell division protein FtsZ

2011 ◽  
Vol 60 (9) ◽  
pp. 1317-1325 ◽  
Author(s):  
Shanmugam Hemaiswarya ◽  
Rohini Soudaminikkutty ◽  
Mohana Lakshmi Narasumani ◽  
Mukesh Doble
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Coli Cell ◽  
Cell Division Protein

scholarly journals An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli

2007 ◽  
Vol 64 (5) ◽  
pp. 1289-1305 ◽  
Author(s):  
Christophe S. Bernard ◽  
Mahalakshmi Sadasivam ◽  
Daisuke Shiomi ◽  
William Margolin
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Cell Division Protein
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