A C-terminal deletion mutant of Mycobacterium tuberculosis FtsZ shows fast polymerization in vitro
Author:
Affiliation:
1. Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore-560012, India
Publisher
Microbiology Society
Subject
Microbiology
Reference23 articles.
1. Reversible unfolding of FtsZ cell division proteins from archaea and bacteria. Comparison with eukaryotic tubulin folding and assembly;Andreu;J Biol Chem,2002
2. Glutamate-induced assembly of bacterial cell division protein FtsZ;Beuria;J Biol Chem,2003
3. FtsZ ring structure associated with division in Escherichia coli;Bi;Nature,1991
4. GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules;Bramhill;Proc Natl Acad Sci U S A,1994
5. Apparent cooperative assembly of the bacterial cell division protein FtsZ demonstrated by isothermal titration calorimetry;Caplan;J Biol Chem,2003
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1. YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli;Molecular Microbiology;2012-05-17
2. A novel membrane-bound toxin for cell division, CptA (YgfX), inhibits polymerization of cytoskeleton proteins, FtsZ and MreB, in Escherichia coli;FEMS Microbiology Letters;2012-01-30
3. YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB;Molecular Microbiology;2010-11-05
4. Bacterial Growth and Cell Division: a Mycobacterial Perspective;Microbiology and Molecular Biology Reviews;2008-03
5. FtsZ: A Novel Target for Tuberculosis Drug Discovery;Current Topics in Medicinal Chemistry;2007-03-01
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