Effect of Ca2+ on the microtubule-severing enzyme p60-katanin. Insight into the substrate-dependent activation mechanism
Version of Record online: 5 MAR 2012
© 2012 The Authors Journal compilation © 2012 FEBS
The FEBS Journal
Volume 279, Issue 7, pages 1339–1352, April 2012
How to Cite
Iwaya, N., Akiyama, K., Goda, N., Tenno, T., Fujiwara, Y., Hamada, D., Ikura, T., Shirakawa, M. and Hiroaki, H. (2012), Effect of Ca2+ on the microtubule-severing enzyme p60-katanin. Insight into the substrate-dependent activation mechanism. The FEBS Journal, 279: 1339–1352. doi: 10.1111/j.1742-4658.2012.08528.x
- Issue online: 16 MAR 2012
- Version of Record online: 5 MAR 2012
- Accepted manuscript online: 11 FEB 2012 10:40AM EST
- (Received 23 August 2011, revised 22 December 2011, accepted 8 February 2012)
Fig. S1. Analyses of the interaction between p60-vMIT and p80-CTD.
Fig. S2. ATPase activity of full-length p60-katanin in the presence of MT, p80-CTD, and increasing concentrations of Ca2+.
Fig. S3.1H-15N HSQC spectra of p60-vMIT in the absence (black) and presence of 5 mM (magenta), 10 mM (cyan), 15 mM (yellow), 25 mM (green) Ca2+.
Fig. S4. Ce3+ titration experiments of p60-vMIT.
Fig. S5. Close-up view of the Ca2+ binding region of p60-katanin in Fig. 6C.
Fig. S6. MT co-sedimentation assay in the presence of p60-katanin and p80-CTD in vitro.
Table S1. The broadened signals of 15N-labeled p60-vMIT in the presence of p80-CTD.
Table S2. Oligonucleotides used as primers for Ala substitution.
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