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Identifier 000426721
Title The role of metacaspases and metacaspase-like complexes in plant physiology
Alternative Title Μελέτη του ρόλου των μετακασπασών και όμοιων συμπλόκων στην φυσιολογία φυτών
Author Χατζηανέστης, Ιωάννης Η.
Thesis advisor Μόσχου, Παναγιώτης
Reviewer Καλαντίδης, Κρίτων
Τζαμαρίας, Δημήτρης
Abstract Proteins are degraded or cleaved into smaller peptides through a catabolic process knows as proteolysis, executed by a large number of proteases. Metacaspases are caspase-like, cysteine-depended proteases found in plants, fungi and protists but not in animals. Their distant homolog, separase, is also a caspase-like protease which shares same proteolytic targets with metacaspases, especially the Plant Elicitor Peptides (PEPs). The plant Arabidopsis has nine metacaspase genes categorized into two types, I (Atmc1 to 3) and II (Atmc4 to 9) based on their structure, and a single separase gene. Despite that many functional studies focused on metacaspases, their physiological role remains elusive due to their genetic and functional redundancy among them. To overcome the genetic and functional redundancy of metacaspases, our lab created a sextuple mutant with the ablation of all type II metacaspases. This mutant showed low germination in long-term stored seeds and was susceptible to salt stress leading us to hypothesize that there is seed coat or seed filling deficiency. In this study, I tested these hypotheses with phenotypic, microscopical and biochemical approaches, by investigating the metacaspase mutant seed coat structure and seed feeling by estimating nitrogen remobilization efficiency to the seed. The metacaspase mutants, however, showed no differences in either seed coat structure or nitrogen remobilization. In addition, I estimated reactive oxygen species (ROS) accumulation in the metacaspase mutant during salt stress, which revealed increased ROS accumulation. I also established vectors for PEP4 and 7, two PEPs especially expressed in the root tip where several metacaspases and separase are expressed, to track spatiotemporal activation of these proteases.
Language English
Subject Arabidopsis
Limited proteolysis
Issue date 2019-11-29
Collection   Faculty/Department--Faculty of Sciences and Engineering--Department of Biology--Post-graduate theses
  Type of Work--Post-graduate theses
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