Identification of a chloroplast ribosomal protein altered by a chloroplast mutation in Chlamydomonas.

Direct evidence is presented that a chloroplast gene mutation in Chlamydomonas reinhardi alters one of the chloroplast ribosomal proteins. Proteins of 30 S subunits of chloroplast ribosomes from mutant strains, carrying maternally inherited antibiotic resistances, were compared with those from the wild type strain by CM-cellulose column chromatography and gel electrophoresis. When 30 S ribosomal proteins from a [3H]arginine-labeled streptomycin-resistant strain and a [14C]arginine-labeled wild type strain, or vice versa, were cochromatographed on a CM-cellulose column, one peak (Peak 17) was absent from the mutant profile. Instead, a pronounced peak was observed to elute at a slightly lower ionic strength than Peak 17 in the region of Peak 16. The molecular weights in both Peak 16 and Peak 17 regions determined by discontinuous sodium dodecyl sulfate polyacrylamide gel electrophoresis were indistinguishable, approximately 18,000. Thus, a chloroplast gene mutation to streptomycin resistance has altered the chromatographic behavior of a chloroplast ribosomal protein of the 30 S subunit. We interpret the additional protein in the mutant eluting at Peak 16 as most likely the mutationally altered form of the Peak 17 protein.