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Nucleic Acids Symposium Series 2000 44(1):7-8; doi:10.1093/nass/44.1.7
© 2000 by Oxford University Press
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Escherichia coli proline tRNA: Structure and recognition sites for prolyl-tRNA synthetase

Tsunemi Hasegawa1,2 and Takashi Yokogawa3,4

1 Department of Material and Biological Chemistry, Faculty of Science, Yamagata University, Yamagata 990-8560, Japan, 2 Institute of Space and Astronautical Science Sagamihara, Kanagawa 229-8510, Japan, 3 Department of Biological Sciences, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Kanagawa 226-8501, Japan, 4 Present address: Department of Biomolecular Science, Faculty of Engineering, Gifu University, Gifu 501-1193, Japan

A major proline tRNA was purified from bulk Escherichia coli A19 tRNA by affinity chromatography with a biotinylated DNA probe. Its nucleotide sequence including modified nucleotides was determined by the post-labelling technique. In order to study the recognition sites of this proline tRNA for prolyl-tRNA synthetase, various mutant transcripts were prepared using an in vitro transcription system with T7 RNA polymerase. Based on the results of in vitro kinetic analyses of mutant transcripts, it was concluded that the second and third letters, G35 and G36, of the anticodon, G37 of the anticodon loop, the discriminator base A73, G72 of the acceptor stem, G49 and U17A that existed in the corner of an L-shaped structure are the recognition sites of proline tRNA for prolyl-tRNA synthetase.


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