Minimal tRNA(Ser) and tRNA(Sec) substrates for human seryl-tRNA synthetase: contribution of tRNA domains to serylation and tertiary structure.
The recognition process of tRNA(Ser) and tRNA(Sec) by human seryl-tRNA synthetase (SerRS) was studied using T7 transcripts representing defined regions of human tRNA(Ser) or tRNA(Sec) and the influence of the tRNA elements on serylation and tertiary structure was elucidated. The anticodon arms of both tRNAs showed no contribution to serylation in contrast to the acceptor stems and the long extra arms. D and T arms were only involved in formation of the L-shaped tRNA structure, not in the recognition process between tRNAs and SerRS. This is the first report of microhelices adapted from human tRNAs being aminoacylated by their homologous synthetase.
Heckl
M
M
Institut für Biochemie, Bayerische Julius-Maximilians-Universität, Biozentrum, Würzburg, Germany.
Busch
K
K
Gross
H J
HJ
D000926:Anticodon; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D009154:Mutation; D009690:Nucleic Acid Conformation; D017434:Protein Structure, Tertiary; D012313:RNA / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D012345:RNA, Transfer, Amino Acid-Specific / Q000737:chemistry / Q000378:metabolism*; D012362:RNA, Transfer, Ser / Q000737:chemistry / Q000378:metabolism*; D012694:Serine / Q000378:metabolism*; D012714:Serine-tRNA Ligase / Q000378:metabolism*
D000926:Anticodon; D012345:RNA, Transfer, Amino Acid-Specific; D012362:RNA, Transfer, Ser; C036928:tRNA, selenocysteine-; D012694:Serine; D012313:RNA; D012714:Serine-tRNA Ligase