In vivo breakdown products of the 32 kDa thylakoid herbicide binding protein. [Spirodela oligorrhiza]

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

OSTI ID:5506240

Greenberg, B M; Mattoo, A K; Gaba, V; Edelman, M

The 32 kDa herbicide binding protein of PSII is degraded rapidly in the light. This phenomenon was investigated in Spirodela oligorrhiza. When fronds were radiolabeled in the presence of cycloheximide only the chloroplast-encoded proteins were labeled. Under these conditions, a breakdown product of 23.5 kDa was observed. This polypeptide was further degraded with kinetics similar to that of the 32 kDa protein. The 23.5 kDa polypeptide cross-reacted with an antibody specific to the 32 kDa protein. By protease digestion it was determined that the 23.5 kDa polypeptide is the intact N-terminal piece of the 32 kDa protein. Thus, this product corresponds to the membrane anchor of the 32 kDa protein. Using the same antibody, breakdown products of 16 kDa, 14 kDa and 12 kDa were observed. These products have also been observed in Zea mays and Solanum nigrum. Using DCMU during pulse-chase experiments at different light intensities, evidence was obtained that the 23.5 kDa breakdown product is generated in vivo.

• Research Organization: Weizmann Institute of Science, Rehovot, Israel
• OSTI ID: 5506240
• 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
ANTI-INFECTIVE AGENTS
ANTIBIOTICS
BIOLOGICAL EFFECTS
CHEMICAL REACTIONS
CYCLOHEXIMIDE
DECOMPOSITION
DRUGS
FUNGICIDES
IN VIVO
LABELLING
ORGANIC COMPOUNDS
PESTICIDES
PHOTOCHEMICAL REACTIONS
PHOTOLYSIS
PHOTOSYNTHESIS
PHOTOSYNTHETIC REACTION CENTERS
PLANTS
PROTEIN STRUCTURE
PROTEINS
SYNTHESIS
WEEDS