Detailed Information on Publication Record
2015
The role of lysine residues on elicitins movement and perception in plants
LOCHMAN, Jan, Michal OBOŘIL, Jitka KLEMPOVÁ, Nikola PTÁČKOVÁ, Zbyněk ZDRÁHAL et. al.Basic information
Original name
The role of lysine residues on elicitins movement and perception in plants
Name (in English)
The role of lysine residues on elicitins movement and perception in plants
Authors
LOCHMAN, Jan, Michal OBOŘIL, Jitka KLEMPOVÁ, Nikola PTÁČKOVÁ and Zbyněk ZDRÁHAL
Edition
SEB Conference 2015, 2015
Other information
Type of outcome
Konferenční abstrakt
Confidentiality degree
není předmětem státního či obchodního tajemství
Změněno: 2/9/2016 08:29, doc. Mgr. Jan Lochman, Ph.D.
Abstract
V originále
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.
Links
GAP501/12/0590, research and development project |
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