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On page 1 showing 1 ~ 2 papers out of 2 papers

Base extrusion is found at helical junctions between right- and left-handed forms of DNA and RNA.

  • Doyoun Kim‎ et al.
  • Nucleic acids research‎
  • 2009‎

Base extrusion is a major structural feature at the junction between B- and Z-DNA (the B-Z junction) where a base pair is broken, and the two bases are extruded from the double helix. Despite the demonstration of base extrusion at the B-Z junction, it is not clear whether a similar base extrusion occurs at other types of junctions involving the left-handed Z conformation. Here, we investigate structural changes of bases at three Z-form junctions: DNA B-Z and Z-Z and RNA A-Z junctions. By monitoring fluorescently labeled duplex nucleic acids using 2-aminopurines at various positions relative to the junction point, we show that base extrusion occurs not only at the DNA B-Z junction, but also at the RNA A-Z and DNA Z-Z junctions. Our data suggest that base extrusion is a general feature of Z-form nucleic-acid junctions.


A left-handed RNA double helix bound by the Z alpha domain of the RNA-editing enzyme ADAR1.

  • Diana Placido‎ et al.
  • Structure (London, England : 1993)‎
  • 2007‎

The A form RNA double helix can be transformed to a left-handed helix, called Z-RNA. Currently, little is known about the detailed structural features of Z-RNA or its involvement in cellular processes. The discovery that certain interferon-response proteins have domains that can stabilize Z-RNA as well as Z-DNA opens the way for the study of Z-RNA. Here, we present the 2.25 A crystal structure of the Zalpha domain of the RNA-editing enzyme ADAR1 (double-stranded RNA adenosine deaminase) complexed to a dUr(CG)(3) duplex RNA. The Z-RNA helix is associated with a unique solvent pattern that distinguishes it from the otherwise similar conformation of Z-DNA. Based on the structure, we propose a model suggesting how differences in solvation lead to two types of Z-RNA structures. The interaction of Zalpha with Z-RNA demonstrates how the interferon-induced isoform of ADAR1 could be targeted toward selected dsRNAs containing purine-pyrimidine repeats, possibly of viral origin.


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