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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
2010-8-16
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1873-3468
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
20
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pubmed:volume |
584
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3533-9
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pubmed:meshHeading |
pubmed-meshheading:20638386-Amino Acid Sequence,
pubmed-meshheading:20638386-Arabidopsis,
pubmed-meshheading:20638386-Arabidopsis Proteins,
pubmed-meshheading:20638386-Crystallography, X-Ray,
pubmed-meshheading:20638386-Genes, Plant,
pubmed-meshheading:20638386-Genetic Complementation Test,
pubmed-meshheading:20638386-Microtubule-Associated Proteins,
pubmed-meshheading:20638386-Models, Molecular,
pubmed-meshheading:20638386-Molecular Chaperones,
pubmed-meshheading:20638386-Molecular Sequence Data,
pubmed-meshheading:20638386-Mutagenesis, Site-Directed,
pubmed-meshheading:20638386-Plants, Genetically Modified,
pubmed-meshheading:20638386-Protein Binding,
pubmed-meshheading:20638386-Protein Folding,
pubmed-meshheading:20638386-Protein Interaction Domains and Motifs,
pubmed-meshheading:20638386-Protein Structure, Secondary,
pubmed-meshheading:20638386-Recombinant Proteins,
pubmed-meshheading:20638386-Sequence Homology, Amino Acid,
pubmed-meshheading:20638386-Tubulin
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pubmed:year |
2010
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pubmed:articleTitle |
Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization.
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pubmed:affiliation |
The National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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