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J. Biol. Chem., Vol. 281, Issue 41, 30697-30706, October 13, 2006

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Structural Analysis of Septin 2, 6, and 7 Complexes^*

From the Center for Cell Signaling, University of Virginia School of Medicine, Charlottesville, Virginia 22908

Mammalian septins comprise a family of 13 genes that encode GTP-binding proteins. Specific combinations of septins can hetero-oligomerize and form filaments in vivo and in vitro, by mechanisms that are not understood. Using fluorescence resonance energy transfer, size exclusion chromatography, and multi-angle light scattering techniques, we have characterized the conformation of a complex of filamentous human septins, Sept2, Sept6, and Sept7. We now show that Sept6 and Sept7 interact through a parallel coiled-coil, and that Sept2 interacts with Sept6 through their C-terminal domains. We have also been able to produce soluble, stable individual septins that behave as rod-like monomers and dimers. Taken together, these observations suggest that polymerized filaments could be comprised of laterally arranged septin core subunits.

Received for publication, May 30, 2006 , and in revised form, August 1, 2006.

^* This work was supported by Grant GM66306 from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Box 800577, HSC, University of Virginia, Charlottesville, VA 22908-0577. Tel.: 434-982-0083; Fax: 434-924-1236; E-mail: ccl3j{at}virginia.edu.

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