Key result
Mg2+ induces HCV IRES IIIabc junction folding into equal antiparallel and parallel species.
Why the study?
The functional importance and dynamic folding behavior of the hepatitis C virus IRES four-way helical junction (IIIabc) in solution were not fully characterized.
The hepatitis C virus IRES four-way junction adopts a dynamic equilibrium of antiparallel and parallel species in the presence of magnesium ions, which may mediate interactions with the ribosome.
Answers are grounded in this paper and cite their sources.
May inform HCV IRES-ribosome dynamics; leaves open functional and therapeutic implications pending in vivo validation.
Translation is initiated within the RNA of the hepatitis C virus at the internal ribosome entry site (IRES). The IRES is a 341-nucleotide element that contains a four-way helical junction (IIIabc) as a functionally important element of the secondary structure. The junction has three additional, nonpaired nucleotides at the point of strand exchange on one diagonal. We have studied the global conformation and folding of this junction in solution, using comparative gel electrophoresis and steady-state and time-resolved fluorescence resonance energy transfer. In the absence of divalent metal ions, the junction adopts an extended-square structure, in contrast to perfect four-way RNA junctions, which retain coaxial helical stacking under all conditions. The IIIabc junction is induced to fold on addition of Mg(2+), by pairwise coaxial stacking of arms, into the conformer in which the unpaired bases are located on the exchanging strands. Fluorescence lifetime measurements indicate that in the presence of Mg(2+) ions, the IIIabc junction exists in a dynamic equilibrium comprising approximately equal populations of antiparallel and parallel species. These dynamic properties may be important in mediating interactions between the IRES and the ribosome and initiation factors.
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Melcher et al. (2003) studied Hepatitis C virus. Mg(2+) addition vs. Absence of divalent metal ions was evaluated on Global conformation and folding of the IIIabc junction. Addition of Mg(2+) induces the hepatitis C virus IRES IIIabc junction to fold into a dynamic equilibrium comprising approximately equal populations of antiparallel and parallel species.
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