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

Lu, Lu ; Nan, Jie LU ; Mi, Wei ; Li, Lan-Fen ; Wei, Chun-Hong ; Su, Xiao-Dong LU and Li, Yi (2010) In FEBS Letters 584(16). p.9-3533
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... (More)

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.

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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
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
in
FEBS Letters
volume
584
issue
16
pages
7 pages
publisher
Wiley-Blackwell
external identifiers
  • pmid:20638386
  • scopus:77955662144
ISSN
1873-3468
DOI
10.1016/j.febslet.2010.07.017
language
English
LU publication?
yes
id
88c0406d-5a12-4137-a2af-387abdfc8bfa
date added to LUP
2016-09-07 22:52:12
date last changed
2022-01-30 05:57:29
@article{88c0406d-5a12-4137-a2af-387abdfc8bfa,
  abstract     = {{<p>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.</p>}},
  author       = {{Lu, Lu and Nan, Jie and Mi, Wei and Li, Lan-Fen and Wei, Chun-Hong and Su, Xiao-Dong and Li, Yi}},
  issn         = {{1873-3468}},
  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}},
  language     = {{eng}},
  month        = {{08}},
  number       = {{16}},
  pages        = {{9--3533}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{FEBS Letters}},
  title        = {{Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization}},
  url          = {{http://dx.doi.org/10.1016/j.febslet.2010.07.017}},
  doi          = {{10.1016/j.febslet.2010.07.017}},
  volume       = {{584}},
  year         = {{2010}},
}