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Besides the consensus that spontaneous conversion of normal cellular PrP\n                    <jats:sup>C<\/jats:sup>\n                    into misfolded and aggregating PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    is the central event in prion disease, an alternative hypothesis suggests the generation of pathological PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    by rare translational frameshifting events in the octa-repeat domain of the PrP mRNA. Ribosomal frameshifting most commonly relies on a slippery site and an adjacent stable RNA structure to stall translating ribosome. Hence, it is crucial to unravel the secondary structure of the octa-repeat domain of PrP mRNA. Each of the five octa-repeats contains a motif (\n                    <jats:underline>GG<\/jats:underline>\n                    C\n                    <jats:underline>GG<\/jats:underline>\n                    U\n                    <jats:underline>GG<\/jats:underline>\n                    U\n                    <jats:underline>GG<\/jats:underline>\n                    CU\n                    <jats:underline>GG<\/jats:underline>\n                    G) which alone\n                    <jats:italic>in vitro<\/jats:italic>\n                    forms a G-quadruplex. Since the propensity of mRNA to form secondary structure depends on the sequence context, we set to determine the structure of the complete octa-repeat region. We assessed the structure of full-length octa-repeat domain of PrP mRNA using dynamic light scattering (DLS), small angle X-ray scattering (SAXS), circular dichroism (CD) spectroscopy and selective 2\u2032-hydroxyl acylation analysis by primer extension (SHAPE). Our data show that the PrP octa-repeat mRNA forms stable A-helical hairpins with no evidence of G-quadruplex structure even in the presence of G-quadruplex stabilizing agents.\n                  <\/jats:p>","DOI":"10.1038\/s41598-019-39213-2","type":"journal-article","created":{"date-parts":[[2019,2,21]],"date-time":"2019-02-21T06:04:12Z","timestamp":1550729052000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes"],"prefix":"10.1038","volume":"9","author":[{"given":"Andreas","family":"Czech","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Petr V.","family":"Konarev","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ingrid","family":"Goebel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dmitri I.","family":"Svergun","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter R.","family":"Wills","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zoya","family":"Ignatova","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2019,2,21]]},"reference":[{"key":"39213_CR1","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1126\/science.6801762","volume":"216","author":"SB Prusiner","year":"1982","unstructured":"Prusiner, S. 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