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首页> 外文期刊>Biochemistry >Zn~(2+)-Induced Rearrangement of the Disordered TPPP/p25 Affects Its Microtubule Assembly and GTPase Activity
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Zn~(2+)-Induced Rearrangement of the Disordered TPPP/p25 Affects Its Microtubule Assembly and GTPase Activity

机译：锌〜（2+）诱导的无序TPPP / p25重排影响其微管组装和GTPase活性。

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Tubulin polymerization promoting protein/p25 (TPPP/p25) modulates the dynamics and stability of the micro-tubule system and plays crucial role in the myelination of oligodendrocytes. Here we showed by CD, fluorescence, and NMR spectroscopies that Zn~(2+) is the first ligand that induces considerable rearrangement of the disordered TPPP/p25. Zinc finger motif (His_2Cvs_2) (His~(610-Cvs~(83)) was identified within the flexible region of TPPP/p25 straddled by extended unstructured N- and C-terminal regions. The specific binding of the Zn~(2+) to TPPP/p25 induced the formation of molten globule but not that of a well-defined tertiary structure. The Zn~(2+)-induced partially folded structure accommodating the zinc binding motif is localized at the single Trp~(76)-containing region as demonstrated by fluorescence resonance energy transfer and quenching experiments. We showed that the Zn~(2+)-induced change in the TPPP/p25 structure modified its interaction with tubulin and GTP coupled with functional consequences: the TPPP/p25-promoted tubulin polymerization was increased while the TPPP/p25-catalyzed GTPase activity was decreased as detected by turbidimetry and by malachite green phosphate release/~(31)P NMR assays, respectively. The finding that the Zn~(2+) of the bivalent cations can uniquely influence physiological relavant interactions significantly contributes to our understanding of the role of Zn~(2+)-related TPPP/p25 processes in the differentiation/myelination of oligodendrocytes possessing a high-affinity Zn~(2+) uptake mechanism.
机译：微管蛋白聚合促进蛋白/ p25（TPPP / p25）调节微管系统的动力学和稳定性，并在少突胶质细胞的髓鞘形成中起关键作用。在这里，我们通过CD，荧光和NMR光谱表明，Zn〜（2+）是第一个引起无序TPPP / p25重排的配体。锌指基序（His_2Cvs_2）（His〜（610-Cvs〜（83））在TPPP / p25的柔性区域中被扩展的非结构化N端和C端区域所包围，Zn〜（2+ ）导致TPPP / p25诱导形成熔融小球，但未形成明确的三级结构，Zn〜（2+）诱导的具有锌结合基序的部分折叠结构位于单个Trp〜（76）-荧光共振能量转移和猝灭实验证实了该区域的存在，我们发现Zn〜（2+）诱导的TPPP / p25结构改变修饰了其与微管蛋白和GTP的相互作用，并伴随了功能性后果：TPPP / p25促进用比浊法和孔雀石绿磷酸盐释放/〜（31）P NMR法检测，微管蛋白的聚合反应增加，而TPPP / p25催化的GTPase活性降低，发现二价阳离子的Zn〜（2+）可以独特地影响生理愉悦相互作用显着有助于我们理解Zn〜（2+）相关的​​TPPP / p25过程在具有高亲和力Zn〜（2+）摄取机制的少突胶质细胞的分化/髓鞘形成中的作用。

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