Identification of a 34 kDa protein altered in the LF-1 mutant as the herbicide-binding D1 protein of photosystem II

Conference · Tue Apr 01 04:00:00 EST 1986 · Plant Physiol.; (United States)

OSTI ID:5383198

Metz, J; Pakrasi, H; Seibert, M; Arntzen, C

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
• Conference Information: Journal Name: Plant Physiol.; (United States) Journal Volume: 80:4
• Country of Publication: United States
• Language: English

Related Subjects

551001* -- Physiological Systems-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ALGAE
BIOLOGICAL FUNCTIONS
CARBON 14 COMPOUNDS
FUNCTIONS
HERBICIDES
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
MICROORGANISMS
MUTANTS
ORGANIC COMPOUNDS
PESTICIDES
PHOTOSYNTHETIC REACTION CENTERS
PHYSIOLOGY
PLANTS
PROTEINS
SCENEDESMUS
STRUCTURAL CHEMICAL ANALYSIS
TRACER TECHNIQUES
UNICELLULAR ALGAE