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 α-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.
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Bariola, P., Retelska, D., Stasiak, A. et al. Remorins form a novel family of coiled coil-forming oligomeric and filamentous proteins associated with apical, vascular and embryonic tissues in plants. Plant Mol Biol 55, 579–594 (2004). https://doi.org/10.1007/s11103-004-1520-4
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DOI: https://doi.org/10.1007/s11103-004-1520-4