GTP/GDP binding stabilizes bacterial cell division protein FtsZ against degradation by FtsH protease in vitro

Srinivasan, Ramanujam and Rajeswari, Haryadi and Bhatt, Brijesh Narayan and Indi, Shantinath and Ajitkumar, Parthasarathi (2007) GTP/GDP binding stabilizes bacterial cell division protein FtsZ against degradation by FtsH protease in vitro. In: Biochemical and Biophysical Research Communications, 357 (1). pp. 38-43.

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Abstract

Factors contributing to the stability of bacterial cell division protein FtsZ remain unknown. In order to identify FtsZ-stabilizing factor(s), we exploited FtsH protease- based in vitro FtsZ degradation assay system. Whole cell lysate from an ftsH-null strain of Escherichia coli inhibited degradation of FtsZ by FtsH in vitro. However, activated charcoal-treated lysate did not inhibit degradation. The loss of ability of the activated charcoal-treated lysate to inhibit degradation of FtsZ was restored when it was replenished with GTP, but not when replenished with other NTPs or dNTPs. The lysate did not protect either FtsZ deletion mutants, which do not bind GTP, or FtsH substrates, $\sigma^{32}$ and cI-108 proteins, against FtsH. GDP and $GTP_\gamma S$ also stabilized FtsZ against FtsH. Neither GTP nor GDP inhibited proteolytic activity of FtsH per se. These observations demonstrate that binding of GTP/GDP ligands is responsible for the proteolytic stability of FtsZ against FtsH.

Item Type:	Journal Article
Publication:	Biochemical and Biophysical Research Communications
Publisher:	Elsevier
Additional Information:	Copyright of this article belongs to Elsevier.
Keywords:	Bacterial cell division protein;FtsZ protein;FtsZ polymers;FtsZ polymerisation;GTP;GDP;FtsH protease
Department/Centre:	Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited:	20 Aug 2007
Last Modified:	19 Sep 2010 04:39
URI:	http://eprints.iisc.ac.in/id/eprint/11725

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