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Selection and Characterization of Artificial Proteins Targeting the Tubulin α Subunit

Abstract : Microtubules are cytoskeletal filaments of eukaryotic cells made of αβ-tubulin heterodimers. Structural studies of non-microtubular tubulin rely mainly on molecules that prevent its self-assembly and are used as crystallization chaperones. Here we identified artificial proteins from an αRep library that are specific to α-tubulin. Turbidity experiments indicate that these αReps impede microtubule assembly in a dose-dependent manner and total internal reflection fluorescence microscopy further shows that they specifically block growth at the microtubule (-) end. Structural data indicate that they do so by targeting the α-tubulin longitudinal surface. Interestingly, in one of the complexes studied, the α subunit is in a conformation that is intermediate between the ones most commonly observed in X-ray structures of tubulin and those seen in the microtubule, emphasizing the plasticity of tubulin. These α-tubulin-specific αReps broaden the range of tools available for the mechanistic study of microtubule dynamics and its regulation.
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Submitted on : Friday, October 22, 2021 - 12:09:34 PM
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Valérie Campanacci, Agathe Urvoas, Tanja Consolati, Soraya Cantos-Fernandes, Magali Aumont-Nicaise, et al.. Selection and Characterization of Artificial Proteins Targeting the Tubulin α Subunit. Structure, Elsevier (Cell Press), 2019, 27 (3), pp.497-506.e4. ⟨10.1016/j.str.2018.12.001⟩. ⟨hal-02123773⟩

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