Reference : Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/6283
Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis.
English
Klahre, U. [> >]
Friederich, Evelyne mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Kost, B. [> >]
Louvard, D. [> >]
Chua, N. H. [> >]
2000
Plant physiology
122
1
35-48
Yes (verified by ORBilu)
International
0032-0889
UNITED STATES
[en] Amino Acid Sequence ; Animals ; Arabidopsis/genetics/metabolism ; Carrier Proteins/genetics/metabolism ; Cercopithecus aethiops ; Microfilament Proteins/genetics/metabolism ; Microscopy, Confocal ; Molecular Sequence Data ; Plant Proteins/genetics/metabolism ; Plants, Toxic ; Sequence Homology, Amino Acid ; Tobacco/cytology/metabolism ; Vero Cells
[en] 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/beta-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.
http://hdl.handle.net/10993/6283

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