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.

Nyckelord

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

Publikations- och innehållstyp

art (ämneskategori)

ref (ämneskategori)