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Recognition nucleotides of Escherichia coli tRNA(Leu) and its elements facilitating discrimination from tRNASer and tRNA(Tyr)
- Source :
- Journal of molecular biology. 231(2)
- Publication Year :
- 1993
-
Abstract
- In order to study how Escherichia coli leucyl-tRNA synthetase recognizes tRNA(Leu) and discriminates it from the other two class II tRNAs, tRNA(Ser) and tRNA(Tyr), various mutations were introduced into class II tRNA transcripts. The discriminator base A73, but not the anticodon sequence, was found to serve as a critical recognition element of tRNA(Leu). A base substitution at the invariant nucleotide A14, but not at any of the other nucleotides characteristic of the E. coli tRNA(Leu) isoacceptors among the three class II tRNAs, caused significantly damaged aminoacylation with leucine. A two base-pair deletion in the long variable arm also resulted in no significant decrease of activity. Transplanting the three tertiary elements characteristic of E. coli tRNA(Leu) (i.e. the location of the G18G19 sequence in the D-loop, the A15 U48 base-pair and the stem pairing pattern of the long variable arm) besides the discriminator base change introduced the leucine charging activity in terms of Vmax/Km, up to 0.1 of that for the normal sequence of tRNA(Leu) into both tRNA(Ser) and tRNA(Tyr). These results indicate that A73 and A14 (or its vicinity) are involved in recognition by leucyl-tRNA synthetase, and that several tertiary elements play a significant role in the discrimination of tRNA(Leu) from the other two class II tRNAs.
- Subjects :
- RNA, Transfer, Leu
DNA Mutational Analysis
Molecular Sequence Data
Aminoacylation
Biology
medicine.disease_cause
Substrate Specificity
Structural Biology
Leucine
medicine
Protein biosynthesis
Escherichia coli
Nucleotide
RNA, Messenger
Molecular Biology
RNA, Transfer, Ser
Sequence Deletion
chemistry.chemical_classification
Mutation
Base Sequence
Nucleotides
Leucine—tRNA ligase
RNA, Transfer, Tyr
Biochemistry
chemistry
Mutagenesis
Protein Biosynthesis
Transfer RNA
Nucleic Acid Conformation
Leucine-tRNA Ligase
Subjects
Details
- ISSN :
- 00222836
- Volume :
- 231
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Journal of molecular biology
- Accession number :
- edsair.doi.dedup.....87eec96fe603e2c65ab38d62afaabf9b