Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization.

Microtubules are composed of polymerized alpha/beta-tubulin heterodimers. Biogenesis of assembly-competent tubulin dimers is a complex multistep process that requires sequential actions of distinct molecular chaperones and cofactors. Tubulin folding cofactor A (TFCA), which captures beta-tubulin during the folding pathway, has been identified in many organisms. Here, we report the crystal ...
structure of Arabidopsis thaliana TFC A (KIESEL, KIS), which forms a monomeric three-helix bundle. The functional binding analysis demonstrated that KIS interacts with beta-tubulin in plant. Furthermore, mutagenesis studies indicated that the alpha-helical regions of KIS participate in beta-tubulin binding. Unlike the budding yeast TFC A, the two loop regions of KIS are not required for this interaction suggesting a distinct binding mechanism of TFC A to beta-tubulin in plants.
Mesh Terms:
Amino Acid Sequence, Arabidopsis, Arabidopsis Proteins, Crystallography, X-Ray, Genes, Plant, Genetic Complementation Test, Microtubule-Associated Proteins, Models, Molecular, Molecular Chaperones, Molecular Sequence Data, Mutagenesis, Site-Directed, Plants, Genetically Modified, Protein Binding, Protein Folding, Protein Interaction Domains and Motifs, Protein Structure, Secondary, Recombinant Proteins, Sequence Homology, Amino Acid, Tubulin
FEBS Lett.
Date: Aug. 20, 2010
Download Curated Data For This Publication
102538
Switch View:
  • Interactions 3