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

• Published in: Biochemical and biophysical research communications Vol. 357; no. 1; pp. 38 - 43
• Main Authors: Srinivasan, Ramanujam, Rajeswari, Haryadi, Bhatt, Brijesh Narayan, Indi, Shantinath, Ajitkumar, Parthasarathi
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 25-05-2007
• Subjects: ATP-Dependent Proteases - metabolism; Bacterial cell division protein; Bacterial Proteins - metabolism; Cell Division - physiology; Cytoskeletal Proteins - metabolism; Escherichia coli; Escherichia coli - cytology; Escherichia coli - metabolism; Escherichia coli Proteins - metabolism; FtsH protease; FtsZ polymerisation; FtsZ polymers; FtsZ protein; GDP; GTP; Guanosine Diphosphate - metabolism; Guanosine Triphosphate - metabolism; Protein Binding; GTP; GDP; FtsZ protein; FtsZ polymerisation; FtsH protease; FtsZ polymers; Bacterial cell division protein
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2007.03.055

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, σ32 and cI-108 proteins, against FtsH. GDP and GTPγS 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.