Abstract tRNAs are key partners in ribosome-dependent protein synthesis. This process is
highly dependent on the fidelity of tRNA aminoacylation by aminoacyl-tRNA synthetases …

Correct expression of the genetic code at translation is directly correlated with tRNA identity.
This survey describes the molecular signals in tRNAs that trigger specific aminoacylations …

The crystal structure of Thermus thermophilus seryl-transfer RNA synthetase, a class 2
aminoacyl-tRNA synthetase, complexed with a single tRNASer molecule was solved at 2.9 Å …

We describe the use of a gel electrophoretic method for measuring the levels of
aminoacylation in vivo of mutant Escherichia coli initiator tRNAs, which are substrates for E …

The archaeal/eukaryotic tyrosyl-tRNA synthetase (TyrRS)–tRNATyr pairs do not cross-react
with their bacterial counterparts. This' orthogonal'condition is essential for using the archaeal …

A list of currently identified gene products of Escherichia coli is given, together with a
bibliography that provides pointers to the literature on each gene product. A scheme to …

General methods for selectively incorporating unnatural amino acids into proteins in vivo,
directly from the growth media, would greatly expand our ability to manipulate protein …

Bacterial tyrosyl‐tRNA synthetases (TyrRS) possess a flexibly linked C‐terminal domain of∼
80 residues, which has hitherto been disordered in crystal structures of the enzyme. We …

THE correct attachment of amino acids to their corresponding (cognate) transfer RNA
catalysed by aminoacyl-tRNA synthetases is a key factor in ensuring the fidelity of protein …

The aminoacyl‐tRNA synthetases are an ancient group of enzymes that catalyze the
covalent attachment of an amino acid to its cognate transfer RNA. The question of specificity …