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Plant Physiol, January 2000, Vol. 122, pp. 35-48
Villin-Like Actin-Binding Proteins Are Expressed Ubiquitously
in Arabidopsis1
Ulrich
Klahre,
Evelyne
Friederich,
Benedikt
Kost,
Daniel
Louvard, and
Nam-Hai
Chua*
Laboratory of Plant Molecular Biology, The Rockefeller University,
1230 York Avenue, New York, New York 10021 (U.K., B.K., N.-H.C.); and
Unité, Mixte de Recherche 144, Laboratoire de Morphogènese
et Signalisation Cellulaires, Institut Curie, 26 rue d'Ulm, Paris
75248, cédex 05, France (E.F., D.L.).
In an attempt to elucidate the
biological function of villin-like actin-binding proteins in plants we
have cloned several genes encoding Arabidopsis proteins with high
homology to animal villin. We found that Arabidopsis contains at least
four villin-like genes (AtVLNs) encoding four different
VLN isoforms. Two AtVLN isoforms are more closely related to mammalian
villin in their primary structure and are also antigenically related,
whereas the other two contain significant changes in the C-terminal
headpiece domain. RNA and promoter/ -glucuronidase expression studies
demonstrated that AtVLN genes are expressed in all
organs, with elevated expression levels in certain types of cells.
These results suggest that AtVLNs have less-specialized functions than
mammalian villin, which is found only in the microvilli of brush border
cells. Immunoblot experiments using a monoclonal antibody against pig
villin showed that AtVLNs are widely distributed in a variety of plant
tissues. Green fluorescent protein fused to full-length AtVLN and
individual AtVLN headpiece domains can bind to both animal and plant
actin filaments in vivo.
1
This paper was supported in part by fellowships
from the Swiss National Science Foundation to U.K. and B.K. and by a
grant from the Department of Energy (no. DOE94ER20143) to N.-H.C.
*
Corresponding author; e-mail chua{at}rockvax.rockefeller.edu; fax
212-327-8327.
© 2000 American Society of Plant Physiologists
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