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SUBSTRATE SPECIFICITY OF A BACTERIAL UV ENDONUCLEASE AND THE OVERLAP WITH IN VITRO PHOTOENZYMATIC REPAIR
Author(s) -
Patrick M. H.,
Harm Helga
Publication year - 1973
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1973.tb06437.x
Subject(s) - pyrimidine dimer , photolyase , endonuclease , polynucleotide , dna , micrococcus luteus , phosphodiester bond , biochemistry , enzyme , biology , bacteriophage , dimer , dna repair , chemistry , stereochemistry , biophysics , escherichia coli , rna , gene , organic chemistry
— The action of an endonuclease from Micrococcus luteus , that operates on ultraviolet (UV) radiation damage, overlaps greatly with that of the yeast photoreactivating enzyme: homo and hetero cyclobutyl pyrimidine dimers in DNA are substrate for both enzymes, but pyrimidine adducts or the ‘spore photoproduct’ in DNA are not. As expected from this overlap, the action of the two enzymes is mutually interfering: single‐strand nicks introduced by the endonuclease effectively preclude photoreactivation; conversely, formation of a photoreactivating enzyme‐dimer complex can prevent nicking by the UV endonuclease. While complex formation between photoreactivating enzyme and dimers in UV‐endonuclease‐treated DNA is apparently normal, the light‐dependent repair step either fails to occur or proceeds at a very low rate. Hence, besides the requirement of a minimum chain length for the function of the photoreactivating enzyme, there is the additional restriction on the position of the dimer in a polynucleotide strand. Finally, rough approximations of the rate constants, k 1 and k 2 , for the UV endonuclease indicate that the in vitro UV‐endonuclease‐dimer complex is relatively unstable, with dissociation of the complex being more probable than hydrolysis of the phosphodiester bond.