PMID:10378004
| Citation |
Sidorkina, OM, Kuznetsov, SV, Blais, JC, Bazin, M, Laval, J and Santus, R (1999) Ultraviolet-B-induced damage to Escherichia coli Fpg protein. Photochem. Photobiol. 69:658-63 |
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| Abstract |
We investigated the effect of UVB light (290 < or = lambda < or = 320 nm) on the structure and enzymatic activities of Escherichia coli Fpg protein (2,6-diamino-4-hydroxy-5N-methylformamidopyrimidine-DNA glycosylase), a DNA repair enzyme containing a zinc finger motif and five chromophoric Trp residues. Irradiation with UVB light of air-saturated pH 7.4 buffered aqueous solutions of Fpg induces the formation of polymers as shown by sodium dodecyl sulfate polyacrylamide gel electrophoretic analysis. In argon-saturated solutions, polymer formation produces a precipitate. The polymerization quantum yield is 0.07 +/- 0.01 and 0.15 +/- 0.02 in air- and argon-saturated solutions, respectively. In the polymerized Fpg protein, second-derivative absorption spectroscopy indicates that three and one Trp residues are destroyed in air- and argon-saturated solutions, respectively. Polymers are devoid of all three activities of the Fpg protein, whereas the unpolymerized protein retains full activities. Matrix-assisted laser desorption/ionization experiments demonstrate that polymer formation is accompanied by the formation of short polypeptides containing the first 32 or 33 residues of the N-terminal domain. Theses polypeptides are most probably formed by the photolytic cleavage of Fpg protein induced by light absorption by the adjacent Trp-34 residue. |
| Links | |
| Keywords |
Amino Acid Sequence; Base Sequence; DNA/chemistry; DNA/radiation effects; DNA-Formamidopyrimidine Glycosylase; Escherichia coli/chemistry; Escherichia coli Proteins; Molecular Sequence Data; N-Glycosyl Hydrolases/chemistry; N-Glycosyl Hydrolases/radiation effects; Photochemistry; Photolysis; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Ultraviolet Rays |
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