Monomerization of pyrimidine dimers in DNA by tryptophan-containing peptides

Wavelength dependence

John C. Sutherland, K. P. Griffin

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

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 languageEnglish (US)
Pages (from-to)529-536
Number of pages8
JournalRadiation Research
Volume83
Issue number3
DOIs
StatePublished - Jan 1 1980
Externally publishedYes

Fingerprint

Pyrimidine Dimers
tryptophan
pyrimidines
Tryptophan
peptides
deoxyribonucleic acid
dimers
Deoxyribodipyrimidine Photo-Lyase
Peptides
DNA
wavelengths
enzymes
Light
Radiation
proteins
lysine
radiation
Cell Extracts
cells
Lysine

ASJC Scopus subject areas

  • Biophysics
  • Radiation
  • Radiology Nuclear Medicine and imaging

Cite this

Monomerization of pyrimidine dimers in DNA by tryptophan-containing peptides : Wavelength dependence. / Sutherland, John C.; Griffin, K. P.

In: Radiation Research, Vol. 83, No. 3, 01.01.1980, p. 529-536.

Research output: Contribution to journalArticle

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