skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Further characterization of ribosome binding to thylakoid membranes. [Pisum sativum]

Abstract

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.

Authors:
;
Publication Date:
Research Org.:
Cornell Univ., Ithaca, NY
OSTI Identifier:
6071002
Resource Type:
Journal Article
Journal Name:
Plant Physiol.; (United States)
Additional Journal Information:
Journal Volume: 84:1
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 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

Citation Formats

Hurewitz, J, and Jagendorf, A T. Further characterization of ribosome binding to thylakoid membranes. [Pisum sativum]. United States: N. p., 1987. Web.
Hurewitz, J, & Jagendorf, A T. Further characterization of ribosome binding to thylakoid membranes. [Pisum sativum]. United States.
Hurewitz, J, and Jagendorf, A T. 1987. "Further characterization of ribosome binding to thylakoid membranes. [Pisum sativum]". United States.
@article{osti_6071002,
title = {Further characterization of ribosome binding to thylakoid membranes. [Pisum sativum]},
author = {Hurewitz, J and Jagendorf, A T},
abstractNote = {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.},
doi = {},
url = {https://www.osti.gov/biblio/6071002}, journal = {Plant Physiol.; (United States)},
number = ,
volume = 84:1,
place = {United States},
year = {Fri May 01 00:00:00 EDT 1987},
month = {Fri May 01 00:00:00 EDT 1987}
}