Nucleic Acids Research, 1989, Vol. 17, No. 19 7855-7863
© 1989
MOLECULAR BIOLOGY |
Role of the extra G-C pair at the end of the acceptor stem of tRNAHb in aminoacylation
Institute of Space and Astronautical Science 3-1-1 Yoshinodai, Sagamihara, Kanagawa 229, Japan 1Department of Life Chemistry, Tokyo Institute of Technology 4259 Nagatsuta, Midori-ku, Yokohama 227, Japan 2Department of Industrial Chemistry, Faculty of Engineering, University of Tokyo Hongo 7-3-1, Bunkyo-ku, Tokyo 113, Japan
*To whom correspondence should be addressed
Received July 11, 1989. Revised August 21, 1989. Accepted August 21, 1989.
All sequenced histidine tRNAs have one additional nucleotide at the 5' end compared with other tRNA species. To Investigate the role of this unique structure in aainoacylation, we constructed in vitro transcripts corresponding to the E. coli histidine tRNA sequence and its variants at the G–1-C73 base pair, by using T7 RNA polymerase transcription systm. A transcript having a wild-type sequence with no modified bases was a good substrate for histidyl-tRNA synthetase (HisRS), and aminoacylation activity was affected by introduction of a triphosphate at the 5' terminus. Base replacements at position 73 caused a marked decrease of Vmax, and deletion and substitution of the G–1 had a remarkable effect on the aminoacylation. A mutant having an A–1-U73 pair was also not a good substrate for HisRS. Comparison among G–1-deficient mutants showed that A was preferable rather than C as the base at position 73. These data demonstrate that the set of the G–1-C73 pair at the end of the acceptor stem of histidine tRNA is crucial for the catalytic process of aminoacylation.
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