PMID:14709061

Citation	Rosen, AE and Musier-Forsyth, K (2004) Recognition of G-1:C73 atomic groups by Escherichia coli histidyl-tRNA synthetase. J. Am. Chem. Soc. 126:64-5
Abstract	This work focuses on the RNA-protein interactions necessary for efficient aminoacylation of tRNAHis by Escherichia coli histidyl-tRNA synthetase (HisRS). The E. coli tRNAHis acceptor stem is characterized by a unique "extra" G-1:C73 base pair. Previous in vivo and in vitro studies showed that G-1:C73 is a major recognition element for E. coli HisRS. To further probe the role of the G-1:C73 base pair in specific aminoacylation, we carried out atomic group "mutagenesis" studies. Systematic base analogue substitutions at the -1:73 position of chemically synthesized microhelixHis substrates suggest that the G-1 base serves to position the 5'-monophosphate, which is critical for aminoacylation. Additionally, the C73 and G-1 bases contain major groove exocyclic atomic groups that contribute to HisRS recognition.
Links	PubMed Online version:10.1021/ja0381609
Keywords	Base Pairing; Escherichia coli/enzymology; Histidine-tRNA Ligase/chemistry; Histidine-tRNA Ligase/metabolism; Nucleic Acid Conformation; RNA, Transfer, Amino Acyl/chemistry; RNA, Transfer, Amino Acyl/metabolism; Substrate Specificity
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