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Review
. 2008 Nov 21;283(47):32153-7.
doi: 10.1074/jbc.R800052200. Epub 2008 Aug 4.

Structure and function of photolyase and in vivo enzymology: 50th anniversary

Affiliations
Review

Structure and function of photolyase and in vivo enzymology: 50th anniversary

Aziz Sancar. J Biol Chem. .
No abstract available

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Figures

FIGURE 1.
FIGURE 1.
Key experiments in photolyase enzymology. A, historical experiment that led to the discovery of photolyase by Rupert et al. (2). This page from C. S. Rupert's notebook is the record of the experiment done on June 16, 1956 and shows repair of UV damage to H. influenzae DNA (TP = transforming principle) by E. coli extract in the presence of blue light. The table shows the results of a Haemophilus transformation assay with UV light-irradiated DNA. The titers of transformants are listed in the last two columns. Row A, unirradiated DNA; row B, irradiated DNA; row D, irradiated DNA mixed with E. coli extract and exposed to blue light; row E, same as in row D but kept in the dark; rows E–I, results from control experiments (2). B, flash photolysis. An E. coli strain dependent exclusively on photolyase for Pyr<>Pyr repair was irradiated with increasing UV doses and either kept in the dark (•) or exposed to a camera flash (○) before plating. Cells exposed to a flash after 1.6 J/m2 have approximately the same survival as cells irradiated with 0.4 J/m2 and kept in dark. Because 1 J/m2 produces 65 Pyr<>Pyr in the E. coli chromosome, this strain must have at least 65 × (1.6–0.4) = 78 photolyase molecules/cell (4).
FIGURE 2.
FIGURE 2.
Structure of photolyase. A, ribbon diagram representation. B, surface potential representation. The dashed box marks the hole leading to FAD. Positively (blue) and negatively (red) charged residues are highlighted.
FIGURE 3.
FIGURE 3.
UV photoproducts and reaction mechanisms of photolyases. A, structures of the two major UV photoproducts. PL, photolyase. B, reaction mechanisms of photolyases. Left, E. coli CPD photolyase; right, D. melanogaster (6-4) photolyase. For clarity, the two critical His residues essential for catalysis by stabilizing the putative oxetane intermediate by the general acid-base mechanism (33, 36) are not shown.

References

    1. Kelner, A. (1949) Proc. Natl. Acad. Sci. U. S. A. 35 73–79 - PMC - PubMed
    1. Rupert, C. S., Goodgal, S. H., and Herriott, R. M. (1958) J. Gen. Physiol. 41 451–471 - PMC - PubMed
    1. Harm, W., Harm, H., and Rupert, C. S. (1968) Mutat. Res. 6 371–385 - PubMed
    1. Sancar, A., and Rupert, C. S. (1978) Gene (Amst.) 4 295–308 - PubMed
    1. Sancar, A. (1994) Biochemistry 33 2–9 - PubMed

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