期刊
BIOCHEMISTRY
卷 50, 期 44, 页码 9568-9578出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi201447w
关键词
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资金
- Hungarian National Scientific Research Fund-OTKA [T-067963, PD-76793, K84271, K72973]
- European Commission [DCI-ALA/19.09.01/10/21526/245-297/ALFA 111(2010)29]
- European Concerted Research Action [COST Action] [TD0905]
- Hungarian Academy of Sciences
- Trans- National EC Research Infrastructure East-NMR at Oxford Facility [228461]
- European Union
- European Social Fund [TAMOP [4.2.1./B-09/KMR-2010-0003]]
Tubulin polymerization promoting protein/p25 (TPPP/p25) modulates the dynamics and stability of the microtubule system and plays crucial role in the myelination of oligodendrocytes. Here we showed by CD, fluorescence, and NMR spectroscopies that Zn2+ is the first ligand that induces considerable rearrangement of the disordered TPPP/p25. Zinc finger motif (His(2)Cys(2)) (His(61)-Cys(83)) was identified within the flexible region of TPPP/p25 straddled by extended unstructured N- and C-terminal regions. The specific binding of the Zn2+ to TPPP/p25 induced the formation of molten globule but not that of a well-defined tertiary structure. The Zn2+-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 Zn2+-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/P-31 NMR assays, respectively. The finding that the Zn2+ of the bivalent cations can uniquely influence physiological relavant interactions significantly contributes to our understanding of the role of Zn2+ uptake TPPP/p25 processes in the differentiation/myelination of oligodendrocytes possessing a high-affinity Zn2+ uptake mechanism.
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