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Nucleic Acids Research, 1992, Vol. 20, No. 15 3911-3917
© 1992

MOLECULAR BIOLOGY

The effect of a unique D-loop structure of a minor tRNAleuUUA from Streptomyces on its structural stability and amino acid accepting activity

Yoshitaka Ueda, Izumi Kumagai* and Kin-ichiro Miura+

Department of Industrial Chemistry, Faculty of Engineering, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113, Japan

*To whom correpondence should be addressed

Received May 26, 1992. Revised July 13, 1992. Accepted July 13, 1992.

Streptomyces bldA gene, which encodes a tRNA corresponding to a very minor leucine codon, UUA, regulates pleiotropic gene expression which is involved in sporulatlon and secondary metabolism. The unique structural feature of this tRNA Is the lack of GG sequence in dihydrouridine loop (D-loop) that generally Is conserved In tRNAs involved in cytoplasmic protein biosynthesis. In order to Investigate the relationship between the D-loop structure and the stability and leucine accepting activity of this tRNA, the wild and Dloop mutant tRNA transcripts were constructed with T7 RNA polymerase In vitro. The wild type tRNALeuUUAshowed the structural stability and leucine accepting activity at physiological temperature for Streptomyces. The E.coli type D-loop mutant, which has a larger loop size and contains a GG doublet, exhibited increased thermostability. The kinetical analyses of the aminoacylation reaction of tRNLeuUUA with S.llvldans and E.coll leucyl-tRNA synthetase (LeuRS) suggest there is a unique recognition mechanism of Streptomyces LeuRS toward tRNAUUALeu.

+Present address: Institute for Biomolecular Science, Gakushuin University, Mejiro, Toshima-ku, Tokyo 171, Japan


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