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Title: Protein methylation reactions in intact pea chloroplasts

Post-translational protein methylation was investigated in Pisum sativum chloroplasts. Intact pea chloroplasts were incubated with ({sup 3}H-methyl)-S-adenosylmethionine under various conditions. The chloroplasts were then separated into stromal and thylakoid fractions and analyzed for radioactivity transferred to protein. Light enhanced the magnitude of labeling in both fractions. One thylakoid polypeptide with an apparent molecular mass of 43 kDa was labeled only in the light. Several other thylakoid and stromal proteins were labeled in both light and dark-labeling conditions. Both base-labile methylation, carboxy-methylesters and base-stable groups, N-methylations were found. Further characterization of the methyl-transfer reactions will be presented.
Authors:
 [1]
  1. (Univ. of Wisconsin, Madison (USA))
Publication Date:
OSTI Identifier:
6957857
Resource Type:
Journal Article
Resource Relation:
Journal Name: Plant Physiology, Supplement; (USA); Journal Volume: 89:4
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; PEAS; PHYSIOLOGY; PROTEINS; METHYLATION; CHLOROPLASTS; LABELLING; TRACER TECHNIQUES; TRITIUM COMPOUNDS; CELL CONSTITUENTS; CHEMICAL REACTIONS; FOOD; HYDROGEN COMPOUNDS; ISOTOPE APPLICATIONS; ORGANIC COMPOUNDS; PLANTS; VEGETABLES 550201* -- Biochemistry-- Tracer Techniques