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Molecular and Cellular Biology, March 2006, p. 1795-1805, Vol. 26, No. 5
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.5.1795-1805.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Nuclear Assembly of UGA Decoding Complexes on Selenoprotein mRNAs: a Mechanism for Eluding Nonsense-Mediated Decay?

Lucia A. de Jesus ,1,{ddagger},§ Peter R. Hoffmann,1,{ddagger} Tanya Michaud,1,¶ Erin P. Forry,1 Andrea Small-Howard,1 Robert J. Stillwell,1 Nadya Morozova,2,|| John W. Harney,2 and Marla J. Berry1*

Department of Cell and Molecular Biology, University of Hawaii at Manoa, Honolulu, Hawaii 96822,1 Thyroid Division, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 021152

Received 28 June 2005/ Returned for modification 27 July 2005/ Accepted 18 November 2005

Recoding of UGA from a stop codon to selenocysteine poses a dilemma for the protein translation machinery. In eukaryotes, two factors that are crucial to this recoding process are the mRNA binding protein of the Sec insertion sequence, SBP2, and the specialized elongation factor, EFsec. We sought to determine the subcellular localization of these selenoprotein synthesis factors in mammalian cells and thus gain insight into how selenoprotein mRNAs might circumvent nonsense-mediated decay. Intriguingly, both EFsec and SBP2 localization differed depending on the cell line but significant colocalization of the two proteins was observed in cells where SBP2 levels were detectable. We identify functional nuclear localization and export signals in both proteins, demonstrate that SBP2 undergoes nucleocytoplasmic shuttling, and provide evidence that SBP2 levels and localization may influence EFsec localization. Our results suggest a mechanism for the nuclear assembly of the selenocysteine incorporation machinery that could allow selenoprotein mRNAs to circumvent nonsense-mediated decay, thus providing new insights into the mechanism of selenoprotein translation.

* Corresponding author. Mailing address: Department of Cell and Molecular Biology, University of Hawaii at Manoa, Honolulu, HI 96822. Phone: (808) 692-1506. Fax: (808) 692-1970. E-mail: mberry{at}hawaii.edu.

{ddagger} These authors contributed equally to this work.

§ Present address: Proteonik, Inc., Gyeonggi Technopark, Rm. 911, Ansan 425-170, South Korea.

Present address: Albany Medical College, 47 New Scotland Ave., Albany, NY 12203.

|| Present address: Department of Biological Sciences, University of Illinois at Chicago, 900 South Ashland Avenue, Chicago, IL 60607.

Molecular and Cellular Biology, March 2006, p. 1795-1805, Vol. 26, No. 5
0022-538X/06/$08.00+0     doi:10.1128/MCB.26.5.1795-1805.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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