Systematic alterations in the anticodon arm make tRNA(Glu)-Suoc a more efficient suppressor.
Open Access
- 1 May 1987
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 6 (5) , 1499-1506
- https://doi.org/10.1002/j.1460-2075.1987.tb02392.x
Abstract
Using site‐specific mutagenesis, we constructed five more efficient variants of tRNA(Glu)‐Suoc, an extremely inefficient ochre suppressor. Each variant has an extended anticodon, or region of the anticodon arm, which is more similar to that found in normal tRNAs which translate codons Uxx. Suppressor efficiency invariably increases with similarity of the extended anticodon to that of a normal Uxx‐translating tRNA. Altered nucleotides in both helix and loop strongly affect efficiency, with no position dependence and no significant interaction between substitutions. The variant with all substitutions is 230‐fold more efficient (in one context) than the parental tRNA(Glu)‐Suoc. Two other unexpected variants seem to be ‘context mutants’, having altered response to message context.This publication has 26 references indexed in Scilit:
- ACETYLORNITHINASE OF ESCHERICHIA COLI: PARTIAL PURIFICATION AND SOME PROPERTIESPublished by Elsevier ,2021
- Effects of surrounding sequence on the suppression of nonsense codonsJournal of Molecular Biology, 1983
- A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragmentsGene, 1982
- A family of cloning vectors containing the lacUV5 promoterGene, 1982
- Construction and characterization of new coliphage M13 cloning vectorsGene, 1980
- Initiator tRNAs have a unique anticodon loop conformation.Proceedings of the National Academy of Sciences, 1979
- Genetic studies of the lac repressorJournal of Molecular Biology, 1979
- Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmidJournal of Bacteriology, 1978
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences, 1977
- Amino acid replacements of the glutamic acid residue at position 48 in the tryptophan synthetase a protein of Escherichia coliJournal of Molecular Biology, 1968