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.

Nan, JieLund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory,Peking University(Swepub:lu)maxl-jna (författare)
Mi, Wei (författare)
Li, Lan-Fen (författare)
Wei, Chun-Hong (författare)
Su, Xiao-DongLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)mbfys-xs (författare)
Li, Yi (författare)
Lunds universitetMAX IV-laboratoriet (creator_code:org_t)

Av författaren/redakt...: Lu, Lu; Nan, Jie; Mi, Wei; Li, Lan-Fen; Wei, Chun-Hong; Su, Xiao-Dong; visa fler...; Li, Yi; visa färre...

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