Selenium is essential to human life and occurs in selenoproteins as selenocysteine (Sec), the 21st amino acid. The selenium atom endows selenocysteine with unique biochemical properties, including a low pK(a) and a high reactivity with many electrophilic agents. Here we describe the introduction of selenocysteine into recombinant non-selenoproteins produced in Escherichia coli, as part of a small tetrapeptide motif at the C terminus. This setenocysteine-containing motif could subsequently be used as a protein tag for purification of the recombinant protein, selenotate-targeted labeling with fluorescent compounds or radiolabeling with either gamma-emitting Se-75 or short-lived positron emitters such as C-11. The results presented here thus show how a wide range of biotechnological applications can be developed starting from the insertion of selenocysteine into proteins.
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