Identification of a 34 kDa protein altered in the LF-1 mutant as the herbicide-binding D1 protein of photosystem II
The LF-1 mutant of Scenedesmus has a complete block on the oxidizing side of its PSII reaction center. However, the reaction center as well as the reducing side of PSII is fully functional in this mutant. Compared to the wildtype (WT) the only detected protein difference in the PSII complex of LF-1 is the change in mobility of a 34 kDa protein to 36 kDa. This protein has been implicated to have a major role in Mn-binding and water-oxidation. The authors have recently shown that photoaffinity labeling of thylakoids with azido-(/sup 14/C)-atrazine tags the 34 kDa protein in WT and the 36 kDa protein in LF-1. It has been shown that the azido-atrazine labeled protein, called D1, functions in herbicide binding and Q/sub A/ to Q/sub B/ electron transfer on the reducing side of PSII. Polyclonal antibodies directed against the D1 protein of Amaranthus hybridus (Ohad, et al., EMBOJ 1985) were found to recognize the Scenedesmus 34 kDa (WT) and 36 kDa (LF-1) proteins. The implied dual function for the D1 protein on the reducing as well as the oxidizing side of PSII reaction center will be discussed.
- Research Organization:
- SERI, Golden, CO
- OSTI ID:
- 5383198
- Journal Information:
- Plant Physiol.; (United States), Vol. 80:4; Conference: Annual meeting of the American Society of Plant Physiologists, Baton Rouge, LA, USA, 8-12 Jun 1986
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
PHOTOSYNTHETIC REACTION CENTERS
STRUCTURAL CHEMICAL ANALYSIS
SCENEDESMUS
PHYSIOLOGY
BIOLOGICAL FUNCTIONS
CARBON 14 COMPOUNDS
HERBICIDES
MUTANTS
PROTEINS
TRACER TECHNIQUES
ALGAE
FUNCTIONS
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
MICROORGANISMS
ORGANIC COMPOUNDS
PESTICIDES
PLANTS
UNICELLULAR ALGAE
551001* - Physiological Systems- Tracer Techniques