Thionin Processing
Abstract
Thionins are antimicrobial peptides which have been isolated from different plant species including cereals and mistletoes. They are usually basic, with a molecular weight around 5 kDa and have a compact structure which is stabilised by 3 or 4 disulfide bridges. Their toxic and antimicrobial activities are probably based on a destruction of cell membranes. Thionins are produced as preproproteins and secreted. The proprotein consists of the thionin and an acidic domain which normally also contains 6 cysteine residues. The aim of this project is to study the processing of the thionin proproteins and the function of the acidic domain. As a first step, the protease responsible for the processing of the proprotein will be purified from barley. The sequence of the protease will then be used to identify the corresponding gene(s) from Arabidopsis (which contains 4 thionin genes). Using mass spectrometry we will study the processing in vitro. Furthermore, mutants or miRNA lines will be used to assess the role of the protease(s) on plant development and on the proprotein in the plant cell. Antibodies will be used to locate the proprotein and the acidic domain in the cell.
keywords arabidopsis antimicrobial peptids proprotein proteinase barley
Publikationen
Project staff
Holger Bohlmann
Assoc. Prof. Dr. Holger Bohlmann
holger.bohlmann@boku.ac.at
Project Leader
01.10.2009 - 30.09.2012