Anand, Syam Prasad and Rajeswari, Haryadi and Gupta, Prabuddha and Srinivasan, Ramanujam and Indi, Shantinath and Ajitkumar, Parthasarathi (2004) A C-terminal deletion mutant of Mycobacterium tuberculosis FtsZ shows fast polymerization in vitro. In: Microbiology, 150 (5). pp. 1119-1121.
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The FtsZ protein forms a dynamic polymeric ring structure, which functions as the guiding scaffold for septal invagination at the mid-cell site during cytokinesis in bacterial cells (Bi & Lutkenhaus, 1991). FtsZ forms polymers in a GTP-dependent manner in vivo and under different cationic conditions in vitro (Andreu et al., 2002; Beuria et al., 2003;Bi & Lutkenhaus, 1991; Bramhill & Thompson, 1994; Caplan & Erickson, 2003; Diaz et al., 2001; Erickson et al., 1996; Lu et al., 1998; Mingorance et al., 2001; Mukherjee & Lutkenhaus, 1994, 1999; Rivas et al., 2000; Romberg et al., 2001; Scheffers et al., 2001; Wang et al., 1997; White et al., 2000; Yu & Margolin, 1997). The rate of polymerization of the FtsZ protein of Mycobacterium tuberculosis H37Rv (MtFtsZ) is remarkably slow when compared to that of the Escherichia coli FtsZ protein (EcFtsZ) (Bramhill & Thompson, 1994; Mukherjee & Lutkenhaus, 1999; White et al., 2000). While polymerization of EcFtsZ reaches steady state in 30 s after the addition of GTP in vitro (Bramhill & Thompson, 1994; Mukherjee & Lutkenhaus, 1999), MtFtsZ takes nearly 10 min to reach the same state (White et al., 2000). The rate of depolymerization of MtFtsZ was also found to be slow, in conformity with its slow GTPase activity (White et al., 2000).
|Item Type:||Journal Article|
|Additional Information:||The copyright belongs to Society for General Microbiology.|
|Department/Centre:||Division of Biological Sciences > Microbiology & Cell Biology|
|Date Deposited:||06 May 2006|
|Last Modified:||19 Sep 2010 04:26|
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