Journal
JOURNAL OF PLANT PHYSIOLOGY
Volume 169, Issue 14, Pages 1329-1339Publisher
ELSEVIER GMBH
DOI: 10.1016/j.jplph.2012.06.010
Keywords
Cold; Heat-shock protein 90; Microtubules; Tobacco; Tubulin
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Funding
- Ministry of Education, Youth and Sports of the Czech Republic [ME10111, LC06034, MSM 0021620858]
- Czech-German DAAD project [D14-CZ 14/2008-09]
- Charles University in Prague GAUK [82710/2010, SVV 265203/2012]
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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 H5p90_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. (c) 2012 Elsevier GmbH. All rights reserved.
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