Identification of an expanded set of translationally active methionine analogues in Escherichia coli
Open Access
- 24 July 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 502 (1-2) , 25-30
- https://doi.org/10.1016/s0014-5793(01)02657-6
Abstract
Amino acid incorporation into proteins in vivo is controlled most stringently by the aminoacyl‐tRNA synthetases. Here we report the incorporation of several new methionine analogues into protein by i...Keywords
This publication has 26 references indexed in Scilit:
- How methionyl-tRNA synthetase creates its amino acid recognition pocket upon l-methionine bindingJournal of Molecular Biology, 2001
- Translational Incorporation of S-Nitrosohomocysteine into ProteinJournal of Biological Chemistry, 2000
- Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific featuresJournal of Molecular Biology, 1999
- Substitution of the methionine residues of calmodulin with the unnatural amino acid analogs ethionine and norleucine: Biochemical and spectroscopic studiesProtein Science, 1999
- High-level Biosynthetic Substitution of Methionine in Proteins by its Analogs 2-Aminohexanoic Acid, Selenomethionine, Telluromethionine and Ethionine in Escherichia coliEuropean Journal of Biochemistry, 1995
- Two separate peptides in Escherichia coli methionyl-tRNA synthetase form the anticodon binding site for methionine tRNABiochemistry, 1993
- Probing Protein Stability with Unnatural Amino AcidsScience, 1992
- Identification of the tRNA anticodon recognition site of Escherichia coli methionyl-tRNA synthetaseBiochemistry, 1990
- Identification of an amino acid region supporting specific methionyl-tRNA synthetase: tRNA recognitionJournal of Molecular Biology, 1989
- Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulfurBiochimica et Biophysica Acta, 1957