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

Lu, Lu (author)
Nan, Jie (author)
Lund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory,Peking University
Mi, Wei (author)
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Li, Lan-Fen (author)
Wei, Chun-Hong (author)
Su, Xiao-Dong (author)
Lund 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
Li, Yi (author)
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 (creator_code:org_t)
2010-07-16
2010
English 7 s.
In: FEBS Letters. - : Wiley. - 1873-3468 .- 0014-5793. ; 584:16, s. 9-3533
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Keyword

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

Publication and Content Type

art (subject category)
ref (subject category)

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