Direct repair of UV-induced DNA lesions represents an elegant method for many organisms to deal with these highly mutagenic and cytotoxic compounds. Although the participating proteins are structurally well investigated, the exact repair mechanism of the photolyase enzymes remains a vivid subject of current research. In this review, we summarize and highlight the recent contributions to this exciting field.
Three for two: by using a Methanosarcina mazei PylRS triple mutant (Y306G, Y384F, I405R) the incorporation of two new exo-norbornene-containing pyrrolysine analogues was achieved. X-ray crystallographic analysis led to the identification of the crucial structural elements involved in substrate recognition by the evolved synthetase.
Klick‐Reaktion mit Nitrilimin: Die speziell evolvierte Pyrrolysyl‐tRNA‐Synthetase von Methanosarcina mazei ermöglicht den Einbau einer Norbornen‐Aminosäure in Proteine in E. coli. Diese Funktionalität kann positionsspezifisch unter physiologischen Bedingungen in einer [3+2]‐ Cycloaddition durch Nitrilimine modifiziert werden (siehe Schema).
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