title: Protein synthesis in plant leaf tissue. The sites of synthesis of the major proteins.
abstract: Protein synthesis in the leaves of green pea seedlings (Pisum sativum) is examined by short term labeling with [35S]methionine and autoradiography of the labeled proteins after fractionation by sodium dodecyl sulfate-acrylamide gel electrophoresis. The two subunits of ribulose-1,5-diphosphate carboxylase and the chloroplast lamellar proteins are identified as the major proteins being synthesized. Three protein chlorophyll complexes are characterized by sodium dodecyl sulfate-acrylamide gel electrophoresis; all three complexes are disrupted by heating to 100 degrees in sodium dodecyl sulfate solution. Studies with inhibitors of protein synthesis indicate that the large subunit of ribulos-1,5-diphosphate carboxylase is synthesized in the chloroplast, in contrast to the majority of the soluble proteins, including the small subunit of ribulose-1,5-diphosphate carboxylase, which is synthesized in the cytoplasm. PII protein, the major lamellar protein associated with photosystem II, is also synthesized on cytoplasmic ribosomes. However, many of the lamellar proteins are synthesized within the chloroplast. Integration into the lamellar system of at least one of the chloroplast-synthesized proteins is shown to be dependent on cytoplasmic protein synthesis.
mesh_terms: D002701:Chloramphenicol / Q000494:pharmacology; D003513:Cycloheximide / Q000494:pharmacology; D008970:Molecular Weight; D010940:Plant Proteins / Q000096:biosynthesis* / Q000302:isolation & purification; D010944:Plants / Q000378:metabolism; D014176:Protein Biosynthesis / Q000187:drug effects
chemical_list: D010940:Plant Proteins; D002701:Chloramphenicol; D003513:Cycloheximide