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

• Published in: Plant molecular biology 2004-07, Vol.55 (4), p.579-594
• Main Authors: Bariola, P, Retelska, D, Stasiak, A, Kammerer, R, Fleming, A, Hijri, M, Frank, S, Farmer, E.E
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; apical meristems; Arabidopsis thaliana; Carrier Proteins - analysis; Carrier Proteins - genetics; Carrier Proteins - ultrastructure; Circular Dichroism; crosslinking; Immunoblotting; immunohistochemistry; leaf primordia; Lycopersicon esculentum - chemistry; Lycopersicon esculentum - genetics; Membrane Proteins - analysis; Membrane Proteins - genetics; Meristem - chemistry; Meristem - genetics; Microscopy, Confocal; Microscopy, Electron; Molecular Sequence Data; Molecular Weight; Oligopeptides - analysis; Oligopeptides - genetics; Phosphoproteins - analysis; Phosphoproteins - genetics; Phosphoproteins - ultrastructure; plant proteins; Plant Proteins - analysis; Plant Proteins - genetics; Plant Proteins - ultrastructure; Plant Roots - chemistry; Plant Roots - genetics; Plant Shoots - chemistry; Plant Shoots - genetics; Plant tissues; Plants - chemistry; Plants - embryology; Plants - genetics; plasma membrane; Potatoes; protein secondary structure; Proteins; Recombinant Proteins - analysis; root tips; shoot meristems; Solanum lycopersicum var. lycopersicum; Solanum tuberosum; Solanum tuberosum - chemistry; Solanum tuberosum - genetics; Tomatoes
• ISSN: 0167-4412; 1573-5028
• DOI: 10.1007/s11103-004-1520-4

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 alpha-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 4.6-7.4 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.