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Molecular and Cellular Biology, March 2002, p. 1402-1411, Vol. 22, No. 5
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.5.1402-1411.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Mammalian Selenoprotein in Which Selenocysteine (Sec) Incorporation Is Supported by a New Form of Sec Insertion Sequence Element

Konstantin V. Korotkov,1 Sergey V. Novoselov,1 Dolph L. Hatfield,2 and Vadim N. Gladyshev1*

Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588,1 Section on the Molecular Biology of Selenium, Basic Research Laboratory, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 208922

Received 31 July 2001/ Returned for modification 10 September 2001/ Accepted 28 November 2001

Selenocysteine (Sec), the 21st amino acid in protein, is encoded by UGA. The Sec insertion sequence (SECIS) element, which is the stem-loop structure present in 3' untranslated regions (UTRs) of eukaryotic selenoprotein-encoding genes, is essential for recognition of UGA as a codon for Sec rather than as a stop signal. We now report the identification of a new eukaryotic selenoprotein, designated selenoprotein M (SelM). The 3-kb human SelM-encoding gene has five exons and is located on chromosome 22 but has not been correctly identified by either Celera or the public Human Genome Project. We characterized human and mouse SelM cDNA sequences and expressed the selenoprotein in various mammalian cell lines. The 3" UTR of the human, mouse, and rat SelM-encoding genes lacks a canonical SECIS element. Instead, Sec is incorporated in response to a conserved mRNA structure, in which cytidines are present in place of the adenosines previously considered invariant. Substitution of adenosines for cytidines did not alter Sec incorporation; however, other mutant structures did not support selenoprotein synthesis, demonstrating that this new form of SECIS element is functional. SelM is expressed in a variety of tissues, with increased levels in the brain. It is localized to the perinuclear structures, and its N-terminal signal peptide is necessary for protein translocation.

* Corresponding author. Mailing address: N151 Beadle Center, Department of Biochemistry, University of Nebraska, Lincoln, NE 68588. Fax: (402) 472-7842. E-mail: vgladyshev1{at}unl.edu.

Molecular and Cellular Biology, March 2002, p. 1402-1411, Vol. 22, No. 5
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.5.1402-1411.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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