Disease relevance of tyrS

• The structural component of the tyrS gene of Escherichia coli, comprising 1269 base pairs, has been fully sequenced by the combined M13/dideoxychain termination approach [1].
• tRNA determinants for transcription antitermination of the Bacillus subtilis tyrS gene [2].
• Two- to threefold enhancement of tyrS expression raised the toxicity 300-fold [3].
• The tyrS genes from Escherichia coli and Bacillus stearothermophilus were toxic to E. coli when they were carried by plasmids with very high copy numbers (pEMBL8 and pEMBL9) [3].

High impact information on tyrS

• A plasmid library of randomly mutated Escherichia coli tyrS (encoding TyrRS) was made by polymerase chain reaction techniques [4].
• The mutant tyrS gene contained a single point mutation resulting in replacement of phenylalanine by serine at position 130 in the protein [4].
• In the first segment, containing sequences homologous to the HIGH consensus, the homology is consistent with the following evolutionary linkage: gltX----glnS----metS----ileS and tyrS [5].
• In the present study, the crystal structures of the Escherichia coli TyrRS catalytic domain, in complexes with l-tyrosine and a l-tyrosyladenylate analogue, Tyr-AMS, were solved at 2.0A and 2.7A resolution, respectively [6].
• This induced-fit form presents a novel "snapshot" of the amino acid activation step in the aminoacylation reaction by TyrRS [6].

Chemical compound and disease context of tyrS

• The desired TyrRS mutants were selected by screening for in vivo azatyrosine incorporation of E. coli cells transformed with the mutant tyrS plasmids [4].
• Point mutations in tyrS that prevent interaction between its product, tyrosyl-tRNA synthetase, and tRNA(Tyr) but do not alter the rate of formation of tyrosyl-adenylate abolished the toxicity [3].

Biological context of tyrS

• Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations [7].
• The tyrosyl-tRNA synthetase from Escherichia coli. Complete nucleotide sequence of the structural gene [1].
• An open reading frame homologous to tyrosyl-tRNA synthetase (tyrS) genes was identified downstream of rpsD but in the opposite orientation [8].
• In the current study, the effect of multiple mutations in tRNA(Tyr) on readthrough of the tyrS leader region terminator, independent of other tRNA functions, was assessed using a system for in vivo expression of pools of tRNA variants; this system may be generally useful for in vivo expression of RNAs with defined end points [2].

Associations of tyrS with chemical compounds

• Expression of a transcriptional tyrS-lacZ fusion was found to be induced by starvation for tyrosine in a tyrosine auxotroph (tyrA1) [9].

Other interactions of tyrS

• Deletion of the terminator region in a tyrS-lacZ fusion resulted in high-level constitutive expression [9].

References