Binding of U1A protein to the 3′ untranslated region of its pre-mRNA 1 1Edited by J. Karn

Autor:	David M.J. Lilley, David Norman, Richard J. Grainger
Rok vydání:	1999
Předmět:	Untranslated region Bimolecular fluorescence complementation Crystallography Förster resonance energy transfer Structural Biology RNA-Protein Interaction Chemistry Three prime untranslated region RNA RNA-binding protein Molecular Biology Fluorescence anisotropy
Zdroj:	Journal of Molecular Biology. 288:585-594
ISSN:	0022-2836
DOI:	10.1006/jmbi.1999.2717
Popis:	We have studied the global structure of the U1A 3' untranslated region (UTR) element using fluorescence resonance energy transfer. Comparison of a single UTR-box with a series of oligoadenine bulges indicates that the UTR-box introduces a significant kink into the axis of the RNA, and quantification of the results suggests an included bend angle of approximately 100 degrees (i.e. 80 degrees from linear). The complete 3'-UTR element is also severely kinked by the two UTR-boxes. We can observe binding of U1A protein to the 3'-UTR element by a change in the fluorescence anisotropy of Cy3 attached to one of the helical ends. In parallel with the binding, we observe a marked increase in fluoresence resonance energy transfer efficiency between fluorophores attached at the two 5' termini, indicating a significant change in global conformation induced by the binding of the protein.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::0b24865fff208639a841ebb6345ef043 https://doi.org/10.1006/jmbi.1999.2717 Zobrazit plný text záznamu Full Text from ScienceDirect