Remorins form a novel family of coiled coil-forming oligomeric and filamentous proteins associated with apical, vascular and embryonic tissues in plants

Details

Serval ID
serval:BIB_F22C9ED79DEA
Type
Article: article from journal or magazin.
Collection
Publications
Title
Remorins form a novel family of coiled coil-forming oligomeric and filamentous proteins associated with apical, vascular and embryonic tissues in plants
Journal
Plant Molecular Biology
Author(s)
Bariola  P.A., Retelska  D., Stasiak  A., Kammerer  R.A., Fleming  A., Hijri  M., Frank  S., Farmer  E.E.
Publication state
Published
Issued date
2004
Volume
55
Pages
579-594
Abstract
Abstract Remorins form a superfamily of plant-specific plasma membrane/lipid raft-associated proteins of unknown structure and function. Using specific antibodies, we localized tomato remorin 1 to apical tissues, leaf primordia and vascular traces. The deduced remorin protein sequence contains a predicted coiled coil domain, suggesting its participation in protein-protein interactions. Circular dichroism revealed that recombinant potato remorin contains an a-helical region that forms a functional coiled coil domain. Electron microscopy of purified preparations of four different recombinant remorins, one from potato, two divergent isologs from tomato, and one from Arabidopsis thaliana, demonstrated that the proteins form highly similar filamentous structures. The diameters of the negatively-stained filaments ranged from 4.6 to 7.4 nm for potato remorin 1, 4.3-6.2 nm for tomato remorin 1, 5.7-7.5 nm for tomato remorin 2, and 5.7-8.0 nm for Arabidopsis Dbp. Highly polymerized remorin 1 was detected in glutaraldehyde-crosslinked tomato plasma membrane preparations and a population of the protein was immunolocalized in tomato root tips to structures associated with discrete regions of the plasma membrane.
Create date
19/11/2007 11:53
Last modification date
20/08/2019 17:19
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