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Structural study of CUG-repeating small RNAs complexed with silencing suppressor P19

dc.contributor.advisorMalinina, Lucy
dc.contributor.authorKatorcha, Elizaveta
dc.contributor.otherBioquímica y Biología Molecular/Biokimika eta Biologia Molekularraes
dc.date.accessioned2014-02-24T15:22:15Z
dc.date.available2014-02-24T15:22:15Z
dc.date.issued2014-02-24T15:22:15Z
dc.date.submitted2012-07-07
dc.identifier.urihttp://hdl.handle.net/10810/11643
dc.description.abstractThe study is focused on structural aspects of interaction between silencing suppressor p19 and CUG-repeating small RNAs. The work involves crystal structure determination of a protein-unbound RNA form and RNA fragments of various lengths (19, 20, 21 nucleotides) complexed with p19-suppressor. Results prove the ability of silencing suppressor p19 to bind CUG-repeating small RNAs, as well as reveal features of U•U mismatches flanked by Watson-Crick C•G base pairs in p19-bound and p19-unbound states. In addition, structural data reveal a p19 specific site for anchoring extra nucleotides in small RNAs. In general, the study extends our knowledge about the mechanism of small RNA recognition by silencing suppressor p19.es
dc.language.isoenges
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectRNAes
dc.subjectprotein-RNA complexes
dc.subjectX-ray crystallographyes
dc.subjectsiRNAes
dc.subjecttrinucleotide repeatses
dc.subjectsilencinges
dc.subjectmismatch base paires
dc.subjectviral suppressores
dc.subjectp19es
dc.subjectCTG/CUG repeatses
dc.subjectstructural biologyes
dc.titleStructural study of CUG-repeating small RNAs complexed with silencing suppressor P19es
dc.typeinfo:eu-repo/semantics/doctoralThesises
dc.rights.holderAttribution-NonCommercial-ShareAlike 4.0 International*
dc.identifier.studentID591943
dc.identifier.projectID658
dc.departamentoesBioquímica y biología moleculares_ES
dc.departamentoeuBiokimika eta biologia molekularraes_ES


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Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 4.0 International