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Originally published In Press as doi:10.1074/jbc.M003215200 on June 19, 2000

J. Biol. Chem., Vol. 275, Issue 35, 27439-27446, September 1, 2000
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Nucleotide-dependent Binding of the GTPase Domain of the Signal Recognition Particle Receptor beta -Subunit to the alpha -Subunit*

Kyle R. Legate, Domina Falcone, and David W. AndrewsDagger

From the Department of Biochemistry, McMaster University, Hamilton, Ontario L8N 3Z5, Canada

The signal recognition particle (SRP) receptor (SR) is a heterodimer of two polypeptides (SRalpha and SRbeta ) that each contain a GTP-binding domain. The GTP-binding domain in the peripheral membrane SRalpha subunit has a well defined role in regulating targeting of SRP-ribosome-nascent chain complexes to the translocon. The only well established function for the transmembrane SRbeta subunit is anchoring SRalpha on the endoplasmic reticulum membrane. Deletion of the amino-terminal transmembrane domain of SRbeta did not affect receptor dimerization, but revealed a cryptic translocation signal that overlaps the GTPase domain. We demonstrate that the domain of SRalpha that binds SRbeta does so by binding directly to the nucleotide-bound form of the GTPase domain of SRbeta . An SRbeta mutant containing an amino acid substitution that allows the GTPase domain to bind XTP dimerized with SRalpha most efficiently in the presence of XTP or XDP, but not ATP. Our results suggest an additional level of regulation of SRP receptor function based on regulated dissociation of the receptor subunits.

* This work was supported by a grant and a scientist award from the Medical Research Council of Canada (to D. W. A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Biochemistry, McMaster University, 1200 Main St. W., Hamilton, Ontario L8N 3Z5, Canada. Tel.: 905-525-9140 (ext. 22075); Fax: 905-522-9033; E-mail: Andrewsd@fhs.mcmaster.ca.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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