Recombinant SEC14-like proteins (TAP) possess GTPase activity |
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Authors: | Daniel Habermehl |
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Institution: | Institute of Biochemistry and Molecular Biology, University of Bern, Bühlstrasse 28, 3012 Bern, Switzerland |
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Abstract: | The three human SEC14-like proteins TAP1, TAP2, and TAP3 were expressed in Escherichia coli and purified by means of an amino-terminal His-tag. The recombinant TAP proteins bound α-, β-, γ-, and δ-tocopherol, certain phospholipids, and squalene. Intriguingly, the TAP proteins showed considerable GTPase activity that was comparable to that of small GTP-binding proteins of the Rab family. Although the TAP proteins contain important motifs to provide GTPase activity, the surrounding secondary structure markedly differed from common G-protein domains. However, these motifs are located in close proximity in the TAP structure and may therefore form an active site for GTP-binding and hydrolysis. |
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Keywords: | SEC14p CRAL-TRIO GTPase Vitamin E Tocopherol Phospholipids |
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