title: Regulatory Proteolysis in Arabidopsis-Pathogen Interactions.
abstract: Approximately two and a half percent of protein coding genes in Arabidopsis encode enzymes with known or putative proteolytic activity. Proteases possess not only common housekeeping functions by recycling nonfunctional proteins. By irreversibly cleaving other proteins, they regulate crucial developmental processes and control responses to environmental changes. Regulatory proteolysis is also indispensable in interactions between plants and their microbial pathogens. Proteolytic cleavage is simultaneously used both by plant cells, to recognize and inactivate invading pathogens, and by microbes, to overcome the immune system of the plant and successfully colonize host cells. In this review, we present available results on the group of proteases in the model plant Arabidopsis thaliana whose functions in microbial pathogenesis were confirmed. Pathogen-derived proteolytic factors are also discussed when they are involved in the cleavage of host metabolites. Considering the wealth of review papers available in the field of the ubiquitin-26S proteasome system results on the ubiquitin cascade are not presented. Arabidopsis and its pathogens are conferred with abundant sets of proteases. This review compiles a list of those that are apparently involved in an interaction between the plant and its pathogens, also presenting their molecular partners when available.
authors.affiliation: Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Herman Ottó út 15, 1022 Budapest, Hungary. pogany.miklos@agrar.mta.hu.
authors.forename: Miklós
authors.initials: M
authors.lastname: Pogány
authors.affiliation: Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Herman Ottó út 15, 1022 Budapest, Hungary. danko.tamas@agrar.mta.hu.
authors.forename: Tamás
authors.initials: T
authors.lastname: Dankó
authors.affiliation: Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Herman Ottó út 15, 1022 Budapest, Hungary. toth.evelin@agrar.mta.hu.
authors.forename: Evelin
authors.initials: E
authors.lastname: Kámán-Tóth
authors.affiliation: Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Herman Ottó út 15, 1022 Budapest, Hungary. schwarczinger.ildiko@agrar.mta.hu.
authors.forename: Ildikó
authors.initials: I
authors.lastname: Schwarczinger
authors.affiliation: Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Herman Ottó út 15, 1022 Budapest, Hungary. bozso.zoltan@agrar.mta.hu.
authors.forename: Zoltán
authors.initials: Z
authors.lastname: Bozsó
mesh_terms: D017360:Arabidopsis / Q000201:enzymology* / Q000382:microbiology / Q000502:physiology; D054884:Host-Pathogen Interactions; D010447:Peptide Hydrolases / Q000378:metabolism*; D010935:Plant Diseases; D057865:Plant Immunity; D010940:Plant Proteins / Q000378:metabolism; D059748:Proteolysis
chemical_list: D010940:Plant Proteins; C053376:pathogenesis-related proteins, plant; D010447:Peptide Hydrolases
keywords: Arabidopsis; Pseudomonas syringae; cell death; effector; immunity; pathogen; protease