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Nucleic Acids Research Advance Access published online on February 7, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn006
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

Solution structure of stem-loop {alpha} of the hepatitis B virus post-transcriptional regulatory element

Martin Schwalbe1, Oliver Ohlenschläger1, Aliaksandr Marchanka1, Ramadurai Ramachandran1, Sabine Häfner1, Tilman Heise2 and Matthias Görlach1,*

1Leibniz-Institut für Altersforschung/Fritz-Lipmann-Institut, Beutenbergstr. 11, D-07745 Jena and 2Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie, Martinistr. 52, D-20251 Hamburg, Germany

*To whom correspondence should be addressed. Tel: +49 3641 656220; Fax: +49 3641 656225; Email: mago{at}fli-leibniz.de

Received October 12, 2007. Revised January 7, 2008. Accepted January 7, 2008.

Chronic hepatitis B virus (HBV) infections may lead to severe diseases like liver cirrhosis or hepatocellular carcinoma (HCC). The HBV post-transcriptional regulatory element (HPRE) facilitates the nuclear export of unspliced viral mRNAs, contains a splicing regulatory element and resides in the 3'-region of all viral transcripts. The HPRE consists of three sub-elements {alpha} (nucleotides 1151–1346), β1 (nucleotides 1347–1457) and β2 (nucleotides 1458–1582), which confer together full export competence. Here, we present the NMR solution structure (pdb 2JYM) of the stem-loop {alpha} (SL{alpha}, nucleotides 1292–1321) located in the sub-element {alpha}. The SL{alpha} contains a CAGGC pentaloop highly conserved in hepatoviruses, which essentially adopts a CUNG-like tetraloop conformation. Furthermore, the SL{alpha} harbours a single bulged G residue flanked by A-helical regions. The structure is highly suggestive of serving two functions in the context of export of unspliced viral RNA: binding sterile alpha motif (SAM-) domain containing proteins and/or preventing the utilization of a 3'-splice site contained within SL{alpha}.

Present address: Martin Schwalbe, Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand. Aliaksandr Marchanka, Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mülheim, Germany. Tilman Heise, Medical University of South Carolina, 173 Ashley Avenue, Charleston SC 29425, USA.


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