Protein synthesis in irradiated cells. I. Ultraviolet radiation.

Excision-deficient haploid yeast cells (Saccharomyces cerevisiae) were exposed to 254-nm UV radiation and protein synthesis inhibition was measured for a large number of different proteins resolved by two-dimensional gel electrophoresis. The derived UV-radiation sensitivities exhibited an overall increase with protein molar mass. Quantitatively, this behavior is compatible with a well known mechanism of transcription inactivation--termination of RNA chains at UV-radiation-induced pyrimidine dimers--if the respective target sizes are inferred from protein molar mass. The observed deviations from the predicted response suggest that (i) UV-radiation damage may also interfere with recognition/binding of RNA polymerase to regulatory sequences and (ii) the frequency of photolesions for a specific protein encoding gene may differ markedly from the mean induction rate for the total yeast genome.