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Molecular and Cellular Biology, December 2006, p. 9177-9184, Vol. 26, No. 24
0270-7306/06/$08.00+0     doi:10.1128/MCB.00856-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Efficient Incorporation of Multiple Selenocysteines Involves an Inefficient Decoding Step Serving as a Potential Translational Checkpoint and Ribosome Bottleneck{triangledown}

Zoia Stoytcheva,1 Rosa M. Tujebajeva,2,{dagger} John W. Harney,2 and Marla J. Berry1*

Department of Cell and Molecular Biology, University of Hawaii at Manoa, Honolulu, Hawaii 96813,1 Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 021152

Received 13 May 2006/ Returned for modification 18 June 2006/ Accepted 15 September 2006

Selenocysteine is incorporated into proteins via "recoding" of UGA from a stop codon to a sense codon, a process that requires specific secondary structures in the 3' untranslated region, termed selenocysteine incorporation sequence (SECIS) elements, and the protein factors that they recruit. Whereas most selenoprotein mRNAs contain a single UGA codon and a single SECIS element, selenoprotein P genes encode multiple UGAs and two SECIS elements. We have identified evolutionary adaptations in selenoprotein P genes that contribute to the efficiency of incorporating multiple selenocysteine residues in this protein. The first is a conserved, inefficiently decoded UGA codon in the N-terminal region, which appears to serve both as a checkpoint for the presence of factors required for selenocysteine incorporation and as a "bottleneck," slowing down the progress of elongating ribosomes. The second adaptation involves the presence of introns downstream of this inefficiently decoded UGA which confer the potential for nonsense-mediated decay when factors required for selenocysteine incorporation are limiting. Third, the two SECIS elements in selenoprotein P mRNA function with differing efficiencies, affecting both the rate and the efficiency of decoding different UGAs. The implications for how these factors contribute to the decoding of multiple selenocysteine residues are discussed.

* Corresponding author. Mailing address: 651 Ilalo Street, Suite 222, Honolulu, HI 96813. Phone: (808) 692-1506. Fax: (808) 692-1968. E-mail: mberry{at}hawaii.edu.

{triangledown} Published ahead of print on 25 September 2006.

{dagger} Present address: Division of Graduate Medical Sciences, Boston University, 715 Huntington Ave., Boston, MA 02118.

Molecular and Cellular Biology, December 2006, p. 9177-9184, Vol. 26, No. 24
0270-7306/06/$08.00+0     doi:10.1128/MCB.00856-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Latreche, L., Jean-Jean, O., Driscoll, D. M., Chavatte, L. (2009). Novel structural determinants in human SECIS elements modulate the translational recoding of UGA as selenocysteine. Nucleic Acids Res 37: 5868-5880 [Abstract] [Full Text]  
  • Gupta, M., Copeland, P. R. (2007). Functional Analysis of the Interplay between Translation Termination, Selenocysteine Codon Context, and Selenocysteine Insertion Sequence-binding Protein 2. J. Biol. Chem. 282: 36797-36807 [Abstract] [Full Text]  
  • Squires, J. E., Stoytchev, I., Forry, E. P., Berry, M. J. (2007). SBP2 Binding Affinity Is a Major Determinant in Differential Selenoprotein mRNA Translation and Sensitivity to Nonsense-Mediated Decay. Mol. Cell. Biol. 27: 7848-7855 [Abstract] [Full Text]  
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