Disordered TPPP/p25 binds GTP and displays Mg2+-dependent GTPase activity

被引：25
|
作者：
Zotter, Agnes [1 ]
Bodor, Andrea [2 ]
Olah, Judit [1 ]
Hlavanda, Emma [1 ]
Orosz, Ferenc [1 ]
Perczel, Andras [2 ,3 ]
Ovadi, Judit [1 ]
机构：
[1] Hungarian Acad Sci, Biol Res Ctr, Inst Enzymol, H-1113 Budapest, Hungary
[2] Eotvos Lorand Univ, Inst Chem, Lab Struct Chem & Biol, H-1117 Budapest, Hungary
[3] Eotvos Lorand Univ, Inst Chem, Prot Modeling Grp HAS ELU, H-1117 Budapest, Hungary
来源：
FEBS LETTERS | 2011年 / 585卷 / 05期
关键词：
Disordered protein; Tubulin Polymerization Promoting Protein/p25; GTP binding; GTP hydrolysis; PROTEIN FUNCTION; TUBULIN; HYDROLYSIS; MECHANISM; DOMAIN; IDENTIFICATION; MICROTUBULES; SUPERFAMILY; ASSEMBLIES; BLOCKS;
D O I：
10.1016/j.febslet.2011.02.006
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码：803 / 808
页数：6
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