Tryptophan-containing peptides and proteins can sensitize the monomerization of pyrimidine dimers in ultraviolet-irradiated DNA; photoreactivating enzymes catalyze the light-induced monomerization of pyrimidine dimers in DNA. It has recently been proposed that a variety of tryptophan-containing proteins and peptide might be confused with true photoreactivating enzymes both in vivo and in vitro. We have thus characterized the wavelength required for the tryptophan-sensitized dimer monomerization to determine if this process is distinguishable from true enzymatic photoreactivation. We find that 313-nm radiation can monomerize pyrimidine dimers in DNA in the presence of the peptide lysyl-tryptophyl-lysine; however, each of these wavelengths is capable of monomerizing dimers in the presence of photoreactivating enzymes. Indeed, 334 and 365 nm are always more effective than 313-nm radiation in the case of true enzymatic photoreactivation. The inability of wavelengths other than those near 300 nm to drive the tryptophan-mediated reaction efficiently is consistent with recently reported spectroscopic experiments. The extreme differences in the wavelength specificities for true enzymatic photoreactivation and tryptophan-sensitized monomerization mean that it is easy to differentiate experimentally between the two phenomena. Consideration of the spectral distributions of conventional sources of 'photoreactivating light' indicate that it is extremely unlikely that any of them could contain significant intensities of the wavelengths required for efficient tryptophan-sensitized monomerization of pyrimidine dimers. We thus conclude that tryptophan-sensitized monomerization cannot account for the disappearance of pyrimidine dimers from DNA cells or cell extracts exposed to photoreactivating light.
|Original language||English (US)|
|Number of pages||8|
|State||Published - Jan 1 1980|
ASJC Scopus subject areas
- Radiology Nuclear Medicine and imaging