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Publication Abstract from PubMed

Microtubules are cytoskeletal filaments of eukaryotic cells made of alphabeta-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 alphaRep library that are specific to alpha-tubulin. Turbidity experiments indicate that these alphaReps 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 alpha-tubulin longitudinal surface. Interestingly, in one of the complexes studied, the alpha 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 alpha-tubulin-specific alphaReps broaden the range of tools available for the mechanistic study of microtubule dynamics and its regulation.

Selection and Characterization of Artificial Proteins Targeting the Tubulin alpha Subunit.,Campanacci V, Urvoas A, Consolati T, Cantos-Fernandes S, Aumont-Nicaise M, Valerio-Lepiniec M, Surrey T, Minard P, Gigant B Structure. 2018 Dec 17. pii: S0969-2126(18)30457-X. doi:, 10.1016/j.str.2018.12.001. PMID:30661854^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.