In vitro polymerization of Mycobacterium leprae FtsZ OR Mycobacterium tuberculosis FtsZ is revived or abolished, respectively, by reciprocal mutation of a single residue
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference31 articles.
1. FtsZ ring structure associated with division in Escherichia coli;Bi;Nature,1991
2. GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubes;Bramhill;Proc. Natl. Acad. Sci. USA,1994
3. Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly;Rivas;J. Biol. Chem.,2000
4. FtsZ dynamics during the division cycle of live Escherichia coli cells;Sun;J. Bacteriol.,1998
5. Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations;Mukherjee;J. Bacteriol.,1999
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1. Mycobacterial FtsZ and inhibitors: a promising target for the anti-tubercular drug development;Molecular Diversity;2023-11-27
2. Unique Biochemical Features of the Cytokinetic Protein FtsZ of Mycobacteria;Mycobacterium - Research and Development;2018-06-20
3. WhmD promotes the assembly of Mycobacterium smegmatis FtsZ: A possible role of WhmD in bacterial cell division;International Journal of Biological Macromolecules;2017-02
4. NDK Interacts with FtsZ and Converts GDP to GTP to Trigger FtsZ Polymerisation - A Novel Role for NDK;PLOS ONE;2015-12-02
5. Mapping Flexibility and the Assembly Switch of Cell Division Protein FtsZ by Computational and Mutational Approaches;Journal of Biological Chemistry;2010-07
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