Advanced

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.

(Less)
Please use this url to cite or link to this publication:
author
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
  • 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
2018-05-29 10:21:54
@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},
  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},
  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},
  volume       = {584},
  year         = {2010},
}