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Nucleic Acids Research, 1994, Vol. 22, No. 15 3124-3130
© 1994

MOLECULAR BIOLOGY

Suppression of the serTA2 mutation with modified tRNASer1 and tRNAfSer5 genes

Yuko Yamada* and Hisayuki Ishikura

Laboratory of Chemistry, Jichi Medical School Minamikawachi-machi, Tochigi 329-04, Japan

* To whom correspondence should be addressed

Received April 11, 1994. Revised June 29, 1994. Accepted June 29, 1994.

Serine tRNA gene derivatives with altered anticodons were introduced to the temperature-sensitive serT42 mutant, whose tRNASer1 shows a base substitution of A10 for wild type G10. When a low copy number vectorsystem was used, the growth and ß-galactosidase synthetic activity of the ser T42 mutant were restored by complementation with the tRNASer5(T34) gene or the tRNASer1 (Q34) gene as well as the tRNASer1 (wt) gene, but not with tRNA (wt), tRNASer5 (A34) or tRNASer1 (G34) genes at 42°C. When multicopy vectors were used, the transformation even with tRNAer (A10) gene restored the growth and 3-galactosidase synthetic activity at 42°C. The tRNA (A10) showed no thermosensitivity in serine acceptor activity by in vitro assay. At 42°C, the amount of tRNAer (A10) in the ser742 mutant was almost the same as those in the wild type. The nucleotides in the tRNAer (A10) were found to be fully modified like those in the wild type tRNA. Both of the tRNAs transcribed from tRNASer1 (T34) and tRNASSer1 (G34) genes showed serine acceptor activity. Modified nucleosides of these tRNAs were also analyzed.


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