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Published online before print March 27, 2008
Protein Science, DOI: 10.1110/ps.083431408
 Copyright © 2008 The Protein Society
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Miranda cargo-binding domain forms an elongated coiled-coil homodimer in solution: Implications for asymmetric cell division in Drosophila

Mohammad S. Yousef1,2,3, Hironari Kamikubo4, Mikio Kataoka4, Ryuichi Kato1, and Soichi Wakatsuki1

1 Structural Biology Research Center, Photon Factory, IMSS, High Energy Accelerator Research Organization, Tsukuba, Ibaraki 305-0801, Japan
2 Biophysics Department, Faculty of Science, Cairo University, Giza, Egypt
3 Center for Advanced Interdisciplinary Sciences (CAIS), Biotechnology Division, Faculty of Science, Cairo University, Giza, Egypt
4 Graduate School of Materials Science, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan

(RECEIVED January 2, 2008; FINAL REVISION February 15, 2008; ACCEPTED February 15, 2008)

Miranda is a multidomain adaptor protein involved in neuroblast asymmetric division in Drosophila melanogaster. The central domain of Miranda is necessary for cargo binding of the neural transcription factor Prospero, the Prospero-mRNA carrier Staufen, and the tumor suppressor Brat. Here, we report the first solution structure of Miranda central "cargo-binding" domain (residues 460–660) using small-angle X-ray scattering. Ab initio modeling of the scattering data yields an elongated "rod-like" molecule with a maximum linear dimension (Dmax) of ~22 nm. Moreover, circular dichroism and cross-linking experiments indicate that the cargo-binding domain is predominantly helical and forms a parallel coiled-coil homodimer in solution. Based on the results, we modeled the full-length Miranda protein as a double-headed, double-tailed homodimer with a long central coiled-coil region. We discuss the cargo-binding capacity of the central domain and propose a structure-based mechanism for cargo release and timely degradation of Miranda in developing neuroblasts.

Keywords: Miranda; Drosophila ; asymmetric cell division; coiled coil; SAXS

Supplemental material: see www.proteinscience.org

Reprint requests to: Mohammad S. Yousef, Structural Biology Research Center, Photon Factory, IMSS, High Energy Accelerator Research Organization, Tsukuba, Ibaraki 305-0801, Japan; e-mail: yousef{at}post.kek.jp; fax: 81-29-879-6179.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.083431408.


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