Tetramerization of human guanylate-binding protein 1 is mediated by coiled-coil formation of the C-terminal α-helices

Syguda A, Bauer M, Benscheid U, Ostler N, Naschberger E, Ince S, Stürzl M, Herrmann C (2012)


Publication Type: Journal article

Publication year: 2012

Journal

Book Volume: 279

Pages Range: 2544-2554

Journal Issue: 14

DOI: 10.1111/j.1742-4658.2012.08637.x

Abstract

The human guanylate-binding protein 1 (hGBP1) is a large GTP-binding protein belonging to the dynamin family, a common feature of which is nucleotide-dependent assembly to homotypic oligomers. Assembly leads to stimulation of GTPase activity, which, in the case of dynamin, is responsible for scission of vesicles from membranes. By yeast two-hybrid and biochemical experiments we addressed intermolecular interactions between all subdomains of hGBP1 and identified the C-terminal subdomain, α12/13, as a new interaction site for self-assembly. α12/13 represents a stable subdomain of hGBP1, as shown by CD spectroscopy. In addition to contacts between GTPase domains leading to dimer formation, the interaction between two α12/13 subdomains, in the course of GTP hydrolysis, results in tetramer formation of the protein. With the help of CD spectroscopy we showed coiled-coil formation of two α12/13 subdomains and concentration-dependent measurements allow estimating a value for the dissociation constant of 7.3 μm. We suggest GTP hydrolysis-driven release of the α12/13 subdomain, making it available for coiled-coil formation. Furthermore, we can demonstrate the biological relevance of hGBP1 tetramer formation in living cells by chemical cross-link experiments. © 2012 FEBS.

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APA:

Syguda, A., Bauer, M., Benscheid, U., Ostler, N., Naschberger, E., Ince, S.,... Herrmann, C. (2012). Tetramerization of human guanylate-binding protein 1 is mediated by coiled-coil formation of the C-terminal α-helices. Febs Journal, 279(14), 2544-2554. https://doi.org/10.1111/j.1742-4658.2012.08637.x

MLA:

Syguda, Adrian, et al. "Tetramerization of human guanylate-binding protein 1 is mediated by coiled-coil formation of the C-terminal α-helices." Febs Journal 279.14 (2012): 2544-2554.

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