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• W1554422725 startingPage "10022" @default.
• W1554422725 abstract "The acceptor helix of histidine tRNAs in Escherichia coli is capped by a unique base pair in which the cytosine at the discriminator position is paired with an extra guanosine at -1. In previous in vitro studies, the presence of the G-1:C73 base pair was found to be required to obtain both optimal histidylation by histidyl-tRNA synthetase and accurate 5' processing by RNase P. We investigated the role of G-1:C73 in histidine tRNA identity and found that nucleotide substitutions conferred mischarging by other amino acids in a pattern that correlated with the discriminator base and not with the extra nucleotide at -1. As shown by primer extension experiments, the relatively minor role of the -1 nucleotide in vivo could be attributed to altered RNase P processing. These studies show that interactions of tRNAs in vivo both with RNase P during tRNA biosynthesis and with the pool of aminoacyl-tRNA synthetases can modulate the effects of substitutions at recognition nucleotides, eliciting changes in transfer RNA identity." @default.
• W1554422725 created "2016-06-24" @default.
• W1554422725 creator A5033892718 @default.
• W1554422725 creator A5079123564 @default.
• W1554422725 date "1994-04-01" @default.
• W1554422725 modified "2023-09-27" @default.
• W1554422725 title "Cytosine 73 is a discriminator nucleotide in vivo for histidyl-tRNA in Escherichia coli" @default.
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• W1554422725 doi "https://doi.org/10.1016/s0021-9258(17)36984-3" @default.
• W1554422725 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8144499" @default.
• W1554422725 hasPublicationYear "1994" @default.
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