Degradation of the 32 kD herbicide binding protein in far red light. [Spirodella oligorrhiza]

Journal Article · Mon Jun 01 00:00:00 EDT 1987 · Plant Physiol.; (United States)

OSTI ID:6071047

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

White light (400-700 nanometers) supports the activity of photosystem I (PSI) and photosystem II while far red light (greater than or equal to700 nanometers) supports PSI almost exclusively. In intact fronds of Spirodela oligorrhiza, turnover of the 32 kilodaltons herbicide binding protein is stimulated under both these light conditions, although not in the dark or at wavelengths > 730 nanometers. As is the case in white light, the far red light induced degradation of the protein is inhibited by DCMU. The means by which far red light operates is unclear. Hypotheses considered include: PSI activated proteolysis, PSI-induced formation of semiquinone anions, and PSI-generated free radicals.

• Research Organization: Weizmann Institute of Science, Rehovat, Israel
• OSTI ID: 6071047
• Journal Information: Plant Physiol.; (United States), Vol. 84:2
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
PHOTOSYNTHETIC MEMBRANES
PROTEOLYSIS
VISIBLE RADIATION
BIOLOGICAL EFFECTS
CATABOLISM
HERBS
LABELLED COMPOUNDS
PHOTOSYNTHESIS
PHYSIOLOGY
PROTEINS
SULFUR 35
TRACER TECHNIQUES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CHEMICAL REACTIONS
DAYS LIVING RADIOISOTOPES
DECOMPOSITION
ELECTROMAGNETIC RADIATION
EVEN-ODD NUCLEI
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
MEMBRANES
METABOLISM
NUCLEI
ORGANIC COMPOUNDS
PHOTOCHEMICAL REACTIONS
PLANTS
RADIATIONS
RADIOISOTOPES
SULFUR ISOTOPES
SYNTHESIS
551001* - Physiological Systems- Tracer Techniques