Cells of Chlamydomonas reinhardtii were pulse-labeled in vivo in the presence of inhibitors of cytoplasmic (anisomycin) or chloroplast (lincomycin) protein synthesis to ascertain the sites of synthesis of chloroplast ribosomal proteins. Fluorographs of the labeled proteins, resolved on two-dimensional (2-D) charge/SDS and one-dimensional (1-D) SDS-urea gradient gels, demonstrated that five to six of the large subunit proteins are products of chloroplast protein synthesis while 26 to 27 of the large subunit proteins are synthesized on cytoplasmic ribosomes. Similarly, 14 of 31 small subunit proteins are products of chloroplast protein synthesis, while the remainder are synthesized in the cytoplasm. The 20 ribosomal proteins shown to be made in the chloroplast of Chlamydomonas more than double the number of proteins known to be synthesized in the chloroplast of this alga.
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1 May 1983
Article|
May 01 1983
Sites of synthesis of chloroplast ribosomal proteins in Chlamydomonas.
R J Schmidt
C B Richardson
N W Gillham
J E Boynton
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1983) 96 (5): 1451–1463.
Citation
R J Schmidt, C B Richardson, N W Gillham, J E Boynton; Sites of synthesis of chloroplast ribosomal proteins in Chlamydomonas.. J Cell Biol 1 May 1983; 96 (5): 1451–1463. doi: https://doi.org/10.1083/jcb.96.5.1451
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