TY - JOUR
T1 - Binding of U1A protein to the 3' untranslated region of its pre-mRNA
AU - Grainger, Richard J.
AU - Norman, David G.
AU - Lilley, David M.J.
N1 - Funding Information:
We thank Dr G. Varani and colleagues for supplying U1A protein, and for valuable discussion. We thank Frank Walter for discussion, and the Cancer Research Campaign and the BBSRC for generous financial support.
PY - 1999/5/14
Y1 - 1999/5/14
N2 - 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°(i.e. 80°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.
AB - 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°(i.e. 80°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.
KW - Fluorescence resonance energy transfer
KW - RNA splicing
KW - RNA-protein interaction
UR - http://www.scopus.com/inward/record.url?scp=0033043229&partnerID=8YFLogxK
U2 - 10.1006/jmbi.1999.2717
DO - 10.1006/jmbi.1999.2717
M3 - Article
C2 - 10329165
AN - SCOPUS:0033043229
VL - 288
SP - 585
EP - 594
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 4
ER -