The Solution Structure of the N-Terminal Domain of Human Tubulin Binding Cofactor C Reveals a Platform for Tubulin Interaction
作者： Mª Flor Garcia-Mayoral , Raquel Castaño , Monica L. Fanarraga , Juan Carlos Zabala , Manuel Rico
DOI: 10.1371/JOURNAL.PONE.0025912
关键词:
摘要: Human Tubulin Binding Cofactor C (TBCC) is a post-chaperonin involved in the folding and assembly of α- β-tubulin monomers leading to release productive tubulin heterodimers ready polymerize into microtubules. In this process it collaborates with other cofactors (TBC's A, B, D, E) forms supercomplex TBCD, β-tubulin, TBCE α-tubulin. Here, we demonstrate that TBCC depletion results multipolar spindles mitotic failure. Accordingly, found at centrosome implicated bipolar spindle formation. We also determine by NMR structure N-terminal domain TBCC. The adopts spectrin-like fold topology composed left-handed 3-stranded α-helix bundle. Remarkably, 30-residue segment flexible disordered solution. This unstructured region interaction tubulin. Our data lead us propose testable model for domain/tubulin recognition which highly charged N-terminus as well residues from three helices loops interact acidic hypervariable regions monomers.
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