Minimal tRNASer and tRNASec substrates for human seryl-tRNA synthetase: contribution of tRNA domains to serylation and tertiary structure
- 15 May 1998
- journal article
- Published by Wiley in FEBS Letters
- Vol. 427 (3) , 315-319
- https://doi.org/10.1016/s0014-5793(98)00435-9
Abstract
The recognition process of tRNASer and tRNASec by human seryl-tRNA synthetase (SerRS) was studied using T7 transcripts representing defined regions of human tRNASer or tRNASec 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 synthetaseKeywords
This publication has 33 references indexed in Scilit:
- Structural and functional considerations of the aminoacylation reactionTrends in Biochemical Sciences, 1997
- The Transfer RNA Identity Problem: a Search for RulesScience, 1994
- Rules that Govern tRNA Identity in Protein SynthesisJournal of Molecular Biology, 1993
- tRNA Structure and Aminoacylation EfficiencyProgress in Nucleic Acid Research and Molecular Biology, 1993
- Recognition of †RNAs by Aminoacyl-†RNA SynthetasesProgress in Nucleic Acid Research and Molecular Biology, 1991
- Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifsNature, 1990
- tRNA IDENTITYAnnual Review of Biochemistry, 1989
- Parameters for the molecular recognition of transfer RNAsBiochemistry, 1989
- Aminoacylation of RNA minihelices with alanineNature, 1989
- A simple structural feature is a major determinant of the identity of a transfer RNANature, 1988