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Nucleic Acids Research, 1994, Vol. 22, No. 12 2217-2221
© 1994

MOLECULAR BIOLOGY

Nuclease resistance of an extraordinarily thermostable mini-hairpin DNA fragment, d(GCGAAGC) and its application to in vitro protein synthesis

Satoko Yoshizawa, Takuya Ueda, Yoshiharu Ishido1, Kin-ichiro Miura2, Kimitsuna Watanabe and Ichiro Hirao1,*

Department of Chemistry and Biotechnology, Faculty of Engineering, The University of Tokyo Hongo, Tokyo 113 1Laboratory of Pharmaceutical Chemistry Tokyo College of Pharmacy, 1432-1, Horinouchi, Hachioji, Tokyo 192-03 2Institute for Biomolecular Science, Gakushuin University Mejiro, Tokyo 171, Japan

*To whom correspondence should be addressed

Received April 12, 1994. Revised May 16, 1994. Accepted May 16, 1994.

The nuclease resistance of a short, thermostable minihairpin, d(GCGAAGC), and other related hairpins was examined. Hairpins possessing a purine-rich (GAA) or (GAAA) loop appeared to be more resistant against nucleases than those with a pyrimidine-rich loop or single-stranded oligomers. Among 8 kinds of oligodeoxyribonucleotides examined, the fragment most resistant against nucleases was a hairpin with the sequence of d(CGCGAAGCG). This hairpin was then utilized for the stabilization of mRNA in an in vitro translation system; the 3'-terminal region of an mRNA was hybridized with an oligodeoxyribonucleotide including the sequence complementary to the 3'-terminus of the mRNA tagged with the nuclease-resistant d(CGCGAAGCG) hairpin sequence. By using this method, dihydrofolate reductase (DHFR) mRNA was stabilized against nucleases contaminating a cell-free translation system of E.coli, with a consequent increase in protein synthesis efficiency of 200%.


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