The role of lysine residues on elicitins movement and perception in plants
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| Year of publication | 2015 |
| Type | Conference abstract |
| Citation | |
| Description | Elicitins are among the most well-known and described oomycetes MAMPs. They are highly conserved sterol-binding proteins containing a 98 amino acid domain secreted by Phytophthora and Pythium spp. which have been shown to induce the hypersensitive response (HR) in several plants. According to their pI elicitins can be separated as either acidic (?, pI<5) or basic (?, pI>7.5). Although ?- and ?-elicitins bind with equivalent affinity to the same high affinity binding site on the plasma membrane, ?-elicitins were shown to be significantly more active in inducing a distal HR and SAR than ? -isoforms. Based on recent findings, the activity of elicitins is not correlated with sterol-binding activity but probably it is dependent on the presence of specific residues when for the effective response the presence of a third interacting component has been assumed. In the present study we investigated the role of individual Lys residues, responsible for the pI of elicitins correlated with their toxicity, on a model of very efficient basic elicitin cryptogein. Our results sustained no principle difference in the perception of acidic and basic elicitins on the plasma membrane but showed significant differences in their movement in plants, especially through the cell walls to the plasma membrane. In this movement the main factors seem to be the presence of specific lysine residues with a proven role in the dimerization process and/or interaction with other partners. |
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