Serpin1 and WSCP differentially regulate the activity of the cysteine protease RD21 during plant development inArabidopsis thaliana.
Proteolytic enzymes (proteases) participate in a vast range of physiological processes, ranging from nutrient digestion to blood coagulation, thrombosis, and beyond. In plants, proteases are implicated in host recognition and pathogen infection, induced defense (immunity), and the deterrence of insect pests. Because proteases irreversibly cleave peptide bonds of protein substrates, their activity must be tightly controlled in time and space. Here, we report an example of how nature evolved alternative mechanisms to fine-tune the activity of a cysteine protease dubbed RD21 (RESPONSIVE TO DESICCATION-21). One mechanism in the model plantArabidopsis thalianastudied here comprises irreversible inhibition of RD21's activity by Serpin1, whereas the other mechanism is a result of the reversible inhibition of RD21 activity by a Kunitz protease inhibitor named water-soluble chlorophyll-binding protein (WSCP). Activity profiling, complex isolation, and homology modeling data revealed unique interactions of RD21 with Serpin1 and WSCP, respectively. Expression studies identified only partial overlaps in Serpin1 and WSCP accumulation that explain how RD21 contributes to the innate immunity of mature plants and arthropod deterrence of seedlings undergoing skotomorphogenesis and greening.
Department of Plant and Environmental Sciences, Clemson University Pee Dee Research and Education Center, Florence, SC 29506; diter@wsu.edu srustgi@clemson.edu sreinbot@ujf-grenoble.fr.|Department of Crop and Soil Sciences, Washington State University, Pullman, WA 99164.
Sachin
S
Rustgi
Laboratoire de Génétique Moléculaire des Plantes and Biologie Environnementale et Systémique, Université Grenoble Alpes, 38041 Grenoble cedex 9, France.|Laboratoire de Biotechnologies Végétales appliquées aux Plantes Aromatiques et Médicinales, Formations de Recherche en Évolution (FRE) CNRS 3727, Université Jean Monnet, 42100 Saint-Étienne, France.
Edouard
E
Boex-Fontvieille
Laboratoire de Génétique Moléculaire des Plantes and Biologie Environnementale et Systémique, Université Grenoble Alpes, 38041 Grenoble cedex 9, France.
Christiane
C
Reinbothe
Department of Crop and Soil Sciences, Washington State University, Pullman, WA 99164; diter@wsu.edu srustgi@clemson.edu sreinbot@ujf-grenoble.fr.
Diter
D
von Wettstein
Laboratoire de Génétique Moléculaire des Plantes and Biologie Environnementale et Systémique, Université Grenoble Alpes, 38041 Grenoble cedex 9, France; diter@wsu.edu srustgi@clemson.edu sreinbot@ujf-grenoble.fr.
Steffen
S
Reinbothe
D017360:Arabidopsis / Q000235:genetics* / Q000254:growth & development / Q000276:immunology / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D001665:Binding Sites; D061146:Chlorophyll Binding Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D057056:Cysteine Proteases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D015870:Gene Expression; D018507:Gene Expression Regulation, Developmental; D018506:Gene Expression Regulation, Plant; D007700:Kinetics; D008958:Models, Molecular; D057865:Plant Immunity / Q000235:genetics; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D054730:Protein Interaction Domains and Motifs; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D036226:Seedlings / Q000235:genetics* / Q000254:growth & development / Q000276:immunology / Q000378:metabolism; D015843:Serpins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D040681:Structural Homology, Protein; D013379:Substrate Specificity
D029681:Arabidopsis Proteins; D061146:Chlorophyll Binding Proteins; D011994:Recombinant Proteins; C549571:Serpin1 protein, Arabidopsis; D015843:Serpins; C576738:WSCP protein, Arabidopsis; D057056:Cysteine Proteases; C549570:RD21 protein, Arabidopsis
RD21; Serpin1; WSCP; protease; protease inhibitor