Further characterization of ribosome binding to thylakoid membranes. [Pisum sativum]
Previous work indicated more polysomes bound to pea (Pisum sativum cv Progress No. 9) thylakoids in light than in the dark, in vivo. With isolated intact chloroplasts incubated in darkness, addition of MgATP had no effect but 24 to 74% more RNA was thylakoid-bound at pH 8.3 than at pH 7. Thus, the major effect of light on ribosome-binding in vivo may be due to higher stroma pH. In isolated pea chloroplasts, initiation inhibitors (pactamycin and kanamycin) decreased the extent of RNA binding, and elongation inhibitors (lincomycin and streptomycin) increased it. Thus, cycling of ribosomes is controlled by translation, initiation, and termination. Bound RNA accounted for 19 to 24% of the total chloroplast RNA and the incorporation of (/sup 3/H)leucine into thylakoids was proportional to the amount of this bound RNA. These data support the concept that stroma ribosomes are recruited into thylakoid polysomes, which are active in synthesizing thylakoid proteins.
- Research Organization:
- Cornell Univ., Ithaca, NY
- OSTI ID:
- 6071002
- Journal Information:
- Plant Physiol.; (United States), Vol. 84:1
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
PHOTOSYNTHETIC MEMBRANES
RIBOSOMES
PROTEINS
BIOSYNTHESIS
BIOLOGICAL RADIATION EFFECTS
CHLOROPLASTS
METABOLISM
PEAS
PH VALUE
PHYSIOLOGY
RNA
TRACER TECHNIQUES
TRITIUM COMPOUNDS
BIOLOGICAL EFFECTS
CELL CONSTITUENTS
FOOD
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
MEMBRANES
NUCLEIC ACIDS
ORGANIC COMPOUNDS
ORGANOIDS
PLANTS
RADIATION EFFECTS
SYNTHESIS
VEGETABLES
551001* - Physiological Systems- Tracer Techniques