Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization.,Lu L, Nan J, Mi W, Li LF, Wei CH, Su XD, Li Y FEBS Lett. 2010 Aug 20;584(16):3533-9. Epub 2010 Jul 16. PMID:20638386[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lu L, Nan J, Mi W, Li LF, Wei CH, Su XD, Li Y. Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization. FEBS Lett. 2010 Aug 20;584(16):3533-9. Epub 2010 Jul 16. PMID:20638386 doi:10.1016/j.febslet.2010.07.017
