Peking Yale Joint Center for Plant Molecular Genetics and Agrobiotechnology

Beijing, China

Peking Yale Joint Center for Plant Molecular Genetics and Agrobiotechnology

Beijing, China

Time filter

Source Type

Lu L.,Peking University | Lu L.,Peking Yale Joint Center for Plant Molecular Genetics and Agrobiotechnology | Nan J.,Peking University | Mi W.,Peking University | And 5 more authors.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications | Year: 2010

Tubulin-folding cofactor A (TFC A) is a molecular post-chaperonin that is involved in the Β-tubulin-folding pathway. It has been identified in many organisms including yeasts, humans and plants. In this work, Arabidopsis thaliana TFC A was expressed in Escherichia coli and purified to homogeneity. After thrombin cleavage, a well diffracting crystal was obtained by the sitting-drop vapour-diffusion method at 289 K. The crystal diffracted to 1.6 Å resolution using synchrotron radiation and belonged to space group I41, with unit-cell parameters a = 55.0, b = 55.0, c = 67.4 Å. © 2010 International Union of Crystallography All rights reserved.


Lu L.,Peking University | Lu L.,Peking Yale Joint Center for Plant Molecular Genetics and Agrobiotechnology | Nan J.,Peking University | Mi W.,Peking University | And 6 more authors.
FEBS Letters | Year: 2010

Microtubules are composed of polymerized α/β-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 β-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 β-tubulin in plant. Furthermore, mutagenesis studies indicated that the α-helical regions of KIS participate in β-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 β-tubulin in plants. © 2010 Federation of European Biochemical Societies.

Loading Peking Yale Joint Center for Plant Molecular Genetics and Agrobiotechnology collaborators
Loading Peking Yale Joint Center for Plant Molecular Genetics and Agrobiotechnology collaborators