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Plant and Cell Physiology Advance Access originally published online on June 27, 2009
Plant and Cell Physiology 2009 50(8):1493-1506; doi:10.1093/pcp/pcp094
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© The Author 2009. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Dynamic Bridges—A Calponin-Domain Kinesin From Rice Links Actin Filaments and Microtubules in Both Cycling and Non-Cycling Cells

Nicole Frey, Jan Klotz and Peter Nick*

Institute of Botany 1 and Center for Functional Nanostructures (CFN), University of Karlsruhe, Kaiserstrasse 2, D-76131 Karlsruhe, Germany

*Corresponding author: E-mail, peter.nick{at}botanik1.uni-karlsruhe.de; Fax, +49-721-608-4193.


  Abstract

Interaction and cross-talk between microtubules and actin microfilaments are important for the cell axis and polarity during plant cell growth and development, but little is known about the molecular components of this interaction. Plant kinesins with a calponin-homology domain (KCHs) were recently identified and associated with a putative role in microtubule–microfilament cross-linking. KCHs belong to a distinct branch of the minus end-directed kinesin subfamily and so far have only been identified in land plants including the mosses. Here we report the identification of a new KCH from rice (Oryza sativa), OsKCH1, and show that OsKCH1 is associated with cortical microtubules and actin microfilaments in vivo. Furthermore, OsKCH1 is shown to bind to micro-tubules and actin microfilaments in vitro in a domain-dependent way. Additionally, this unique type of kinesin is shown to oligomerize both in vivo and in vitro. These findings are discussed with respect to a general role for KCHs as linkers between actin filaments and microtubules in both cell elongation and division.

Keywords: Actin filaments - KCH - Microtubules - Plant kinesins - Rice

Abbreviations: AMP-PNP, 5'-adenylylimidodiphosphate; BiFC, bimolecular fluorescence complementation; CH domain, calponin-homology domain; FABDP2, fimbrin actin-binding domain 2; GFP, green fluorescent protein; MBD-MAP4, microtubule-binding domain of microtubule-associated protein 4; OsKCH1, Oryza sativa kinesin with a calponin-homology domain 1; RFP, red fluorescent protein; SEC, size exclusion chromatography; TRITC, tetramethyl-rhodamine isothiocyanate; YFP, yellow fluorescent protein.

(Received April 28, 2009; Accepted June 25, 2009)
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