NDLI: Effect of G-1 on histidine tRNA microhelix conformation

Content Provider	PubMed Central
Author	Seetharaman, Mahadevan Williams, Caroline Cramer, Christopher J. Karin, Musier-forsyth
Copyright Year	2003
Abstract	Histidine tRNAs (tRNAHis) are unique in that they possess an extra 5′-base (G-1) not found in other tRNAs. Deletion of G-1 results in at least a 250-fold reduction in the rate of histidine charging in vitro. To better understand the role of the G-1 nucleotide in defining the structure of tRNAHis, and to correlate structure with cognate amino acid charging, NMR and molecular dynamics (MD) studies were performed on the wild-type and a ΔG-1 mutant Escherichia coli histidine tRNA acceptor stem microhelix. Using NMR-derived distance restraints, global structural characteristics are described and interpreted to rationalize experimental observations with respect to aminoacylation activity. The quality of the NMR-derived solution conformations of the wild-type and ΔG-1 histidine microhelices (micro helixHis) is assessed using a variety of MD-based computational protocols. Most of the duplex regions of the acceptor stem and the UUCG tetraloop are well defined and effectively superimposable for the wild-type and ΔG-1 mutant microhelixHis. Differences, however, are observed at the end of the helix and in the single-stranded CCCA-3′ tail. The wild-type microhelixHis structure is more well defined than the mutant and folds into a ‘stacked fold-back’ conformation. In contrast, we observe fraying of the first two base pairs and looping back of the single-stranded region in the ΔG-1 mutant resulting in a much less well defined conformation. Thus the role of the extra G-1 base of the unique G-1:C73 base pair in tRNAHis may be to prevent end-fraying and stabilize the stacked fold-back conformation of the CCCA-3′ region.
Related Links	http://dx.doi.org/10.1093/nar/gkg930
Ending Page	7321
Page Count	11
Starting Page	7311
File Format	PDF
ISSN	13624962
e-ISSN	13624962
Journal	Nucleic Acids Research
Issue Number	24
Volume Number	31
Language	English
Publisher	Oxford University Press
Publisher Date	2003-12-15
Access Restriction	Open
Rights Holder	Oxford University Press
Subject Keyword	Genetics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics

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