Modification of herbicide binding to photosystem II in two biotypes of Senecio vulgaris L

• Published in: Plant physiology (Bethesda) Vol. 64; no. 6; pp. 995 - 999
• Main Authors: Pfister, Klaus, Radosevich, Steven R., Arntzen, Charles J.
• Format: Journal Article
• Language: English
• Published: United States American Society of Plant Physiologists 01.12.1979
• Subjects: Binding sites; Chemical suspensions; Chloroplasts; Herbicide resistance; Herbicides; Molecules; Photosystem II; Plants; Thylakoids; Triazines
• ISSN: 0032-0889; 1532-2548
• DOI: 10.1104/pp.64.6.995

The present study compares the binding and inhibitory activity of two photosystem II inhibitors: 3-(3,4-dichlorophenyl)-1,1-dimethylurea (diuron [DCMU]) and 2-chloro-4-(ethylamine)-6-(isopropyl amine)-s-triazene (atrazine). Chloroplasts isolated from naturally occurring triazine-susceptible and triazine-resistant biotypes of common groundsel (Senecio vulgaris L.) showed the following characteristics. (a) Diuron strongly inhibited photosynthetic electron transport from H2O to 2,6-dichlorophenolindophenol in both biotypes. Strong inhibition by atrazine was observed only with the susceptible chloroplasts. (b) Hill plots of electron transport inhibition data indicate a noncooperative binding of one inhibitor molecule at the site of action for both diuron and atrazine. (c) Susceptible chloroplasts show a strong diuron and atrazine binding (14C-radiolabel assays) with binding constants (K) of 1.4 × 10-8 molar and 4 × 10-8 molar, respectively. In the resistant chloroplasts the diuron binding was slightly decreased (K = 5 × 10-8 molar), whereas no specific atrazine binding was detected. (d) In susceptible chloroplasts, competitive binding between radioactively labeled diuron and non-labeled atrazine was observed. This competition was absent in the resistant chloroplasts. We conclude that triazine resistance of both intact plants and isolated chloroplasts of Senecio vulgaris L. is based upon a minor modification of the protein in the photosystem II complex which is responsible for herbicide binding. This change results in a specific loss of atrazine (triazine)-binding capacity.