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To study incorporation of nonproteinogenic amino acids in bacterial proteome we performed a global, unbiased protein modification analysis of the E. coli K12 strain with defective editing mechanism of the leucyl tRNA synthetase (LeuRS), which in addition to leucine incorporates a nonproteinogenic am...
ORGANISM(S): Escherichia coli 
2016-07-11 | PXD003468 | Pride
Aminoacyl-tRNA synthetases (aaRSs), the enzymes responsible for coupling tRNAs to their cognate amino acids, minimize translational errors by intrinsic hydrolytic editing. Here, we compared the propensity of norvaline (Nva), a linear amino acid not coded for protein synthesis, to the proteinogenic, ...
ORGANISM(S): Escherichia coli 
2019-01-28 | PXD011051 | Pride
The stringent response was defined in Lactococcus lactis through transcript profiling after the addition of a chemical inductor, the norvaline. Gene expression was measured in the exponential growth phase (reference sample) and at 1.6 h after norvaline addition. Four hundred and sixty one differenti...
ORGANISM(S): Lactococcus lactis 
The stringent response was defined in Lactococcus lactis through transcript profiling after the addition of a chemical inductor, the norvaline. Gene expression was measured in the exponential growth phase (reference sample) and at 1.6 h after norvaline addition. Four hundred and sixty one differenti...
ORGANISM(S): Lactococcus lactis 
2009-04-28 | GSE10254 | GEO
Correct pairing of amino acids and tRNA is prerequisite for correct translation of genetic information during protein biosynthesis. Here, we present effects of proteome-wide isoleucine mistranslation in Escherichia coli induced by editing-defective isoleucyl-tRNA synthetase (IleRS). Two types of mis...
ORGANISM(S): Escherichia Coli 
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