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- W2014177596 abstract "The disordered Tubulin Polymerization Promoting Protein/p25 (TPPP/p25) modulates the dynamics and stability of the microtubule system and plays a crucial role in differentiation of oligodendrocytes. Here we first demonstrated by multinuclear NMR that the extended disordered segments are localized at the N- and C-terminals straddling a flexible region. We showed by affinity chromatography, fluorescence spectroscopy and circular dichroism that GTP binds to TPPP/p25 likely within the flexible region; neither positions nor intensities of the peaks in the assigned terminals were affected by GTP. In addition, we demonstrated that TPPP/p25 specifically hydrolyses GTP in an Mg2+-dependent manner. The GTPase activity is comparable with the intrinsic activities of small G proteins suggesting its potential role in multiple physiological processes." @default.
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- W2014177596 date "2011-02-11" @default.
- W2014177596 modified "2023-09-27" @default.
- W2014177596 title "Disordered TPPP/p25 binds GTP and displays Mg<sup>2+</sup> -dependent GTPase activity" @default.
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- W2014177596 doi "https://doi.org/10.1016/j.febslet.2011.02.006" @default.
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