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

Research output: Contribution to journalArticle

Abstract

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.

Details

Authors
  • Lu Lu
  • Jie Nan
  • Wei Mi
  • Lan-Fen Li
  • Chun-Hong Wei
  • Xiao-Dong Su
  • Yi Li
Organisations
External organisations
  • Peking University
Research areas and keywords

Keywords

  • 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
Original languageEnglish
Pages (from-to)3533-9
Number of pages7
JournalFEBS Letters
Volume584
Issue number16
Publication statusPublished - 2010 Aug 20
Publication categoryResearch
Peer-reviewedYes