γ-Tubulin has a conserved intrinsic property of self-polymerization into double stranded filaments and fibrillar networks

Publication date: Available online 27 February 2018 Source:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research Author(s): Jana Chumová, Lucie Trögelová, Hana Kourová, Jindřich Volc, Vadym Sulimenko, Petr Halada, Ondřej Kučera, Oldřich Benada, Anna Kuchařová, Anastasiya Klebanovych, Pavel Dráber, Geoffrey Daniel, Pavla Binarová γ-Tubulin is essential for microtubule nucleation and also plays less understood roles in nuclear and cell-cycle-related functions. High abundancy of γ-tubulin in acentrosomal Arabidopsis cells facilitated purification and biochemical characterization of large molecular species of γ-tubulin. TEM, fluorescence, and atomic force microscopy of purified high molecular γ-tubulin forms revealed the presence of linear filaments with a double protofilament substructure, filament bundles and aggregates. Filament formation from highly purified γ-tubulin free of γ-tubulin complex proteins (GCPs) was demonstrated for both plant and human γ-tubulin. Moreover, γ-tubulin associated with porcine brain microtubules formed oligomers. Experimental evidence on the intrinsic ability of γ-tubulin to oligomerize/polymerize was supported by conservation of α- and β-tubulin interfaces for longitudinal and lateral interactions for γ-tubulins. STED (stimulated emission depletion) microscopy of Arabidopsis cells revealed fine, short γ-tubulin fibrillar structures enriched on mitotic microtubular arrays that accumulated at polar reg...
Source: Biochimica et Biophysica Acta (BBA) Molecular Cell Research - Category: Molecular Biology Source Type: research