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Molecular and Cellular Biology, March 2006, p. 2337-2346, Vol. 26, No. 6
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.6.2337-2346.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Supramolecular Complexes Mediate Selenocysteine Incorporation In Vivo

Andrea Small-Howard,1 Nadya Morozova,2,{dagger} Zoia Stoytcheva,1 Erin P. Forry,1 John B. Mansell,2,{ddagger} John W. Harney,2 Bradley A. Carlson,3 Xue-ming Xu,3 Dolph L. Hatfield,3 and Marla J. Berry1*

Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, Hawaii 96822,1 Thyroid Division, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115,2 Laboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 208923

Received 23 October 2005/ Returned for modification 21 December 2005/ Accepted 4 January 2006

Selenocysteine incorporation in eukaryotes occurs cotranslationally at UGA codons via the interactions of RNA-protein complexes, one comprised of selenocysteyl (Sec)-tRNA[Ser]Sec and its specific elongation factor, EFsec, and another consisting of the SECIS element and SECIS binding protein, SBP2. Other factors implicated in this pathway include two selenophosphate synthetases, SPS1 and SPS2, ribosomal protein L30, and two factors identified as binding tRNA[Ser]Sec, termed soluble liver antigen/liver protein (SLA/LP) and SECp43. We report that SLA/LP and SPS1 interact in vitro and in vivo and that SECp43 cotransfection increases this interaction and redistributes all three proteins to a predominantly nuclear localization. We further show that SECp43 interacts with the selenocysteyl-tRNA[Ser]Sec-EFsec complex in vitro, and SECp43 coexpression promotes interaction between EFsec and SBP2 in vivo. Additionally, SECp43 increases selenocysteine incorporation and selenoprotein mRNA levels, the latter presumably due to circumvention of nonsense-mediated decay. Thus, SECp43 emerges as a key player in orchestrating the interactions and localization of the other factors involved in selenoprotein biosynthesis. Finally, our studies delineating the multiple, coordinated protein-nucleic acid interactions between SECp43 and the previously described selenoprotein cotranslational factors resulted in a model of selenocysteine biosynthesis and incorporation dependent upon both cytoplasmic and nuclear supramolecular complexes.

* Corresponding author. Mailing address: Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, HI 96822. Phone: (808) 956-5811. Fax: (808) 956-5855. E-mail: mberry{at}hawaii.edu.

{dagger} Present address: Department of Biological Sciences, University of Illinois at Chicago, 900 South Ashland Ave., Chicago, IL 60607.

{ddagger} Present address: A. J. Park, Intellectual Property Lawyers and Consultants, Wellington, New Zealand.

Molecular and Cellular Biology, March 2006, p. 2337-2346, Vol. 26, No. 6
0022-538X/06/$08.00+0     doi:10.1128/MCB.26.6.2337-2346.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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