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Nucleic Acids Research, 1991, Vol. 19, No. 5 1113-1119
© 1991

MOLECULAR BIOLOGY

Inhibition of translation initiation by antisense oligonucleotides via an RNase-H independent mechanism

Claudine Boiziau1,+, Robin Kurfurst2, Christian Cazenave1,§, Victoria Roig2, Nguyen T. Thuong2 and Jean-Jacques Toulmé1,2,*

1Laboratoire de Biophysique, Muséum National d'Histoire Naturelle 43 rue Cuvier, 75005 Paris 2Centre de Biophysique Moléculaire CNRS, 45071 Orléans Cedex 02, France

* To whom correspondence should be addressed at Laboratoire de Biophysique, Université de Bordeaux II, Bât. 3a, 146 rue Léo Saignat, 33076 Bordeaux Cedex, France

Received October 8, 1990. Revised February 3, 1991. Accepted February 3, 1991.

We have used {alpha}oligomers as antisense oligonucleotides complementary to three different sequences of the rabbit ß-globin mRNA: a region adjacent to the cap site, a region spanning the AUG initiation codon or a sequence in the coding region. These {alpha}oligonucleotides were synthesized either with a free 5' OH group or linked to an acrldine derivative. The effect of these oligonucleotides on mRNA translation was investigated in cell-free extracts and in Xenopus oocytes. In rabbit reticulocyte lysate and in wheat germ extracts oligomers targeted to the cap site and the initiation codon reduced ß-globin synthesis in a dose-dependent manner, whereas the target mRNA remained intact. The anti-cap {alpha}oligomer was even more efficient that its ß-counterpart in rabbit reticulocyte lysate. In contrast, only the {alpha}-oligomer,linked to the acridine derivatives, complementary to the cap region displayed significant antisense properties in Xenopuse oocytes. Therefore initiation of translation can be arrested by oligonucleotide/RNA hybrids which are not substrates for RNase-H.

+Present addresses: Laboratoire de Biophysique Moléculaire, Université de Bordeaux, 33076 Bordeaux Cedex, France

§Present addresses: Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA


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