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JXB Advance Access published online on January 6, 2009
Journal of Experimental Botany, doi:10.1093/jxb/ern307
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© 2009 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

Tobacco Arp3 is localized to actin-nucleating sites in vivo

Jan Maisch1,*, Jindriska Fiserová2, Lukás Fischer2 and Peter Nick1

1Institute of Botany 1, University of Karlsruhe, Kaiserstraße 2, D-76128 Karlsruhe, Germany
2Department of Plant Physiology, Faculty of Science, Charles University, Vinicná 5, Prague 2, 128 44 Czech Republic

* To whom correspondence should be addressed. E-mail: jan.maisch{at}bio.uni-karlsruhe.de

The polarity of actin is a central determinant of intracellular transport in plant cells. To visualize actin polarity in living plant cells, the tobacco homologue of the actin-related protein 3 (ARP3) was cloned and a fusion with the red fluorescent protein (RFP) was generated. Upon transient expression of these fusions in the tobacco cell line BY-2 (Nicotiana tabacum L. cv. Bright Yellow 2), punctate structures were observed near the nuclear envelope and in the cortical plasma. These dots could be shown to decorate actin filaments by expressing RFP–ARP3 in a marker line, where actin was tagged by GFP (green fluorescent protein)–FABD (fimbrin actin-binding domain 2). When actin filaments were disrupted by latrunculin B or by prolonged cold treatment, and subsequently allowed to recover, the actin filaments reformed from the RFP–ARP3 structures, that therefore represented actin nucleation sites. The intracellular distribution of these sites was followed during the formation of pluricellular files, and it was observed that the density of RFP–ARP3 increased in the apex of the polarized, terminal cells of a file, whereas it was equally distributed in the central cells of a file. These findings are interpreted in terms of position-dependent differences of actin organization.

Key words: Actin, actin-related protein 3 (ARP3), tobacco BY-2

Received 2 September 2008; Revised 23 October 2008 Accepted 7 November 2008


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