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.
- MeSH
- benzochinony farmakologie MeSH
- fylogeneze MeSH
- makrocyklické laktamy farmakologie MeSH
- mikrotubuly účinky léků metabolismus MeSH
- molekulární sekvence - údaje MeSH
- polymerizace účinky léků MeSH
- proteiny tepelného šoku HSP90 chemie izolace a purifikace metabolismus MeSH
- rekombinantní proteiny izolace a purifikace metabolismus MeSH
- repetitivní sekvence aminokyselin MeSH
- rostlinné proteiny metabolismus MeSH
- rýže (rod) účinky léků metabolismus MeSH
- sekvence aminokyselin MeSH
- tabák cytologie účinky léků metabolismus MeSH
- transport proteinů účinky léků MeSH
- tubulin metabolismus MeSH
- vazba proteinů účinky léků MeSH
- zelené fluorescenční proteiny metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
