Published online 16 March 2004
Nucleic Acids Research, 2004, Vol. 32, No. 5 1746-1755
© 2004 Oxford University Press
Secondary structure and stability of the selenocysteine insertion sequences (SECIS) for human thioredoxin reductase and glutathione peroxidase
1 Division of Molecular Structure, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK, 2 James Graham Brown Cancer Center, University of Louisville, 529 S. Jackson Street, Louisville, KY 40202, USA, 3 Department of Chemistry, University of Louisville, 2320 S. Brook Street, Louisville, KY 40208, USA and 4 Department of Land, Air and Water Resources, University of California, One Shields Avenue, Davis, CA 95616-8627, USA
*To whom correspondence should be addressed. Tel: +1 502 852 6448; Fax: +1 502 852 8149; Email: teresa.fan{at}louisville.edu
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
We have used high resolution NMR and thermodynamics to characterize the secondary structure and stability of the selenocysteine insertion sequences (SECIS) of human glutathione peroxidase (58 nt) and thioredoxin reductase (51 nt). These sequences are members of the two classes of SECIS recently identified with two distinct structures capable of directing selenocysteine incorporation into proteins in eukaryotes. UV melting experiments showed a single cooperative and reversible transition for each RNA, which indicates the presence of stable secondary structures. Despite their large size, the RNAs gave well resolved NMR spectra for the exchangeable protons. Using NOESY, the imino protons as well as the cytosine amino protons of all of the Watson–Crick base pairs were assigned. In addition, a number of non-canonical base pairs including the wobble G.U pairs were identified. The interbase-pair NOEs allowed definition of the hydrogen-bonded structure of the oligonucleotides, providing an experimental model of the secondary structure of these elements. The derived secondary structures are consistent with several features of the predicted models, but with some important differences, especially regarding the conserved sequence motifs.
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