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Identifier 000419705
Title Μελέτη πρωτεϊνών του εκκριτικού συστήματος τύπου ΙΙΙ στο φυτοπαθογόνο Pseudomonas syringae pv phaseolicola
Alternative Title Study of proteins of type III secretion system in plant pathogen Pseudomonas syringae pv phaseolicola
Author Λαγκουβάρδος, Μιχάλης Ε.
Thesis advisor Καλαντίδης, Κρίτων
Reviewer Κοκκινίδης, Μιχαήλ
Αϊβαλιώτης, Μιχαήλ
Abstract Interaction between pathogenic bacteria and their host has been an important research field over the last years. The first genes coding for parts of a very complex secretory machine was first described in the late 90s. This machine was named type III secretion system and it had the ability upon contacting a target cell (host) to trigger the transfer of virulence factors directly from the bacterial to the eukaryotic cytoplasm. As far as plant cells are concerned, type III secretion is also able to surpass the plant cell wall. The cur-rent study emphasized in two proteins of the type III secretory machine of the plant pathogenic bacterium Pseudomonas syringae pv phaseolicola, which causes halo blight of the common bean Phaseolus vulgaris. In particular, the proteins HrpO and HrpE that are thought to make a complex with each other were studied. In addition, these proteins have homology with proteins FliJ and FliH of the flagellum. FliJ has a chaperone activi-ty and FliH is a negative regulator of the ATPase. These two proteins have been found to interact. The plasmid vector pET26b was used for the creation of a bicistronic vector that had HrpO/HrpE in line (along with a His – tag in HrpE) and one vector expressing the HrpO gene. The bicistronic vector was used for the transformation of Escherichia coli bacterial cells and the under evaluation complex was isolated successfully. Subse-quently, circular dichroism experiments were held in order to collect structural data for the isolated complex. In addition, structural data were also collected from isolated HrpO and HrpE. Results showed that a) the two proteins form a complex that can be success-fully isolated by Ni – NTA agarose column and b) the complex and both the proteins isolated separately show high percentage of a – helical conformation. In conclusion, we assume that the two proteins we studied form a complex which is unstable. That com-plex can cause structural conformations in both HrpO and HrpE when it is formed.
Language Greek
Subject Circular dichroism
Complex
HrpE
HrpO
Type III secretion system
Κυκλικός δι-χρωισμός
Σύμπλοκο
Issue date 2018-11-23
Collection   Faculty/Department--Faculty of Sciences and Engineering--Department of Biology--Post-graduate theses
  Type of Work--Post-graduate theses
Permanent Link https://elocus.lib.uoc.gr//dlib/7/9/8/metadata-dlib-1543579491-305092-31209.tkl Bookmark and Share
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