Abstract
Microtubules (MTs) are essential for many processes in plant cells. MT-associated proteins (MAPs) influence MT polymerization dynamics and enable them to perform their functions. The molecular chaperone Hsp90 has been shown to associate with MTs in animal and plant cells. However, the role of Hsp90-MT binding in plants has not yet been investigated. Here, we show that Hsp90 associates with cortical MTs in tobacco cells and decorates MTs in the phragmoplast. Further, we show that tobacco Hsp90_MT binds directly to polymerized MTs in vitro. The inhibition of Hsp90 by geldanamycin (GDA) severely impairs MT re-assembly after cold-induced de-polymerization. Our results indicate that the plant Hsp90 interaction with MTs plays a key role in cellular events, where MT re-organization is needed.
Copyright © 2012 Elsevier GmbH. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Benzoquinones / pharmacology
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Green Fluorescent Proteins / metabolism
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HSP90 Heat-Shock Proteins / chemistry
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HSP90 Heat-Shock Proteins / isolation & purification
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HSP90 Heat-Shock Proteins / metabolism*
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Lactams, Macrocyclic / pharmacology
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Microtubules / drug effects
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Microtubules / metabolism*
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Molecular Sequence Data
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Nicotiana / cytology
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Nicotiana / drug effects
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Nicotiana / metabolism*
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Oryza / drug effects
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Oryza / metabolism*
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Phylogeny
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Plant Proteins / metabolism*
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Polymerization / drug effects
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Protein Binding / drug effects
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Protein Transport / drug effects
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Repetitive Sequences, Amino Acid
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Tubulin / metabolism
Substances
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Benzoquinones
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HSP90 Heat-Shock Proteins
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Lactams, Macrocyclic
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Plant Proteins
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Recombinant Proteins
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Tubulin
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Green Fluorescent Proteins
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geldanamycin