Selected article for: "SUD core and zone interference"
Author: Tan, Jinzhi; Vonrhein, Clemens; Smart, Oliver S.; Bricogne, Gerard; Bollati, Michela; Kusov, Yuri; Hansen, Guido; Mesters, Jeroen R.; Schmidt, Christian L.; Hilgenfeld, Rolf
Title: The SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-Quadruplexes
  • Document date: 2009_5_15
    • ID: 1aqt65cc_19
    Snippet: As there is no evidence for SARS-CoV Nsp3 entering the nucleus and binding to DNA, we examined whether SUD would bind to an RNA known to form a quadruplex structure. Indeed, zone-interference gel shift experiments revealed major shifts for both SUD and SUD core in the presence of the oligoribonucleotide 59-UGGGGGGAGGGAGGGAGGGA-39, which is a proteinbinding element in the 39-nontranslated region of chicken elastin mRNA [34] and forms G-quadruplexe.....
    Document: As there is no evidence for SARS-CoV Nsp3 entering the nucleus and binding to DNA, we examined whether SUD would bind to an RNA known to form a quadruplex structure. Indeed, zone-interference gel shift experiments revealed major shifts for both SUD and SUD core in the presence of the oligoribonucleotide 59-UGGGGGGAGGGAGGGAGGGA-39, which is a proteinbinding element in the 39-nontranslated region of chicken elastin mRNA [34] and forms G-quadruplexes [35] ( Figure 4C ). Furthermore, we observed a significant gel shift for SUD core when we added the short oligonucleotide UGGGGU, which has also been shown to form a G-quadruplex ( [36] ; PDB code 1J8G). This shift was also enhanced by the addition of K + ( Figure 4D ). Thus, SUD binds RNA (rG)-quadruplexes and DNA (dG)-quadruplexes with comparable affinity.

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