Nucleic Acids Research, 1994, Vol. 22, No. 25 5709-5716
© 1994
Articles |
A guanosine quadruplex and two stable hairpins flank a major cleavage site in insulin-like growth factor II mRNA
Department of Biological Chemistry, Institute of Molecular Biology, University of Copenhagen S0lvgade 83 H, DK-1307 Copenhagen K 1Department of Clinical Biochemistry, University Hospital Rigshospitalet DK-2100 Copenhagen 0Ø, Denmark
*To whom correspondence should be addressed
Received August 9, 1994. Revised November 15, 1994. Accepted November 15, 1994.
Insulin-like growth factor II (IGF-II) mRNAs are cleaved by an endonucleolytlc event in a conserved part of their 3' untranslated region that is predicted to exhibit a complex higher-order RNA structure. In the present study, we have examined the putative secondary structures of In vitro transcripts from the conserved part of human and rat mRNAs by enzymatic and chemical probing. The results show that the cleavage site Is situated between two highly structured domains. The upstream domain consists of two large hairpins, whereas the downstream domain Is guanoslne-rlch. The guanoslne-rich domain adopts a compact unimolecular conformation in Na+ or K+ but not in Li +, and It completely arrests reverse transcription in K+ but only partially in Na +, Indicating the presence of an intramolecular guanosine quadruplex. The flanking higher-order structures may ensure that the cleavage site is not sequestered In stable RNA structures, thus allowing interactions with RNA or proteins at posttranscrlptlonal stages of IGF-II expression.
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