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Radioactivity is incorporated essentially exclusively into ribosomal protein when [3H] tetracycline is irradiated in the presence of ribosomes. Such incorporation is shown to arise from three different processes: photoincorporation of native tetracycline, photoincorporation of tetracycline photoproduct, and, in the absence of P-mercaptoethanol, light-independent incorporation of tetracycline photoproduct. When both the rate of tetracycline to tetracycline photoproduct conversion and the protein labeling pattern produced by tetracycline photoproduct (utilizing both polyacrylamide gel electrophoresis and specific immunoprecipitation) are determined separately, it is possible to subtract out the contribution of tetracycline photoproduct to the overall labeling pattern obtained on irradiation of tetracycline and ribosomes and thus determine the labeling pattern due to native tetracycline incorporation. In this way we show that protein S7 is the major protein labeled by native tetracycline in both the presence and absence of @-mercaptoethanol. High labeling of proteins S18 and S4

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