ArticleNucleic acids research2001
Importance of the conserved nucleotides around the tRNA-like structure of Escherichia coli transfer-messenger RNA for protein tagging.
Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Novel Genomic and Evolutionary Perspective of Cyanobacterial tRNAs.Frontiers in genetics · 2017Article
- tmRNA-mediated trans-translation as the major ribosome rescue system in a bacterial cell.Frontiers in genetics · 2014Review
- Mechanism of trans-translation revealed by in vitro studies.Frontiers in microbiology · 2014Review
- A second eukaryotic group with mitochondrion-encoded tmRNA: in silico identification and experimental confirmation.RNA biology · 2013Article
- tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation.Journal of nucleic acids · 2011Article
- Role of the C-terminal tail of SmpB in the early stage of trans-translation.RNA (New York, N.Y.) · 2010Article
- Article
- A functional interaction of SmpB with tmRNA for determination of the resuming point of trans-translation.RNA (New York, N.Y.) · 2007Article
- Structure probing of tmRNA in distinct stages of trans-translation.RNA (New York, N.Y.) · 2007Article
- In vitro trans-translation of Thermus thermophilus: ribosomal protein S1 is not required for the early stage of trans-translation.RNA (New York, N.Y.) · 2007Article
- Comparative 3-D modeling of tmRNA.BMC molecular biology · 2005Article
- A minimum structure of aminoglycosides that causes an initiation shift of trans-translation.Nucleic acids research · 2004Article
- SmpB functions in various steps of trans-translation.Nucleic acids research · 2002Article
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
A bacterial RNA functioning as both tRNA and mRNA, transfer-messenger RNA (tmRNA) rescues stalled ribosomes and clears the cell of incomplete polypeptides. For function, Escherichia coli tmRNA requires an elaborate interplay between a tRNA-like structure and an internal mRNA domain that are connected by a 295 nt long compact secondary structure. The tRNA-like structure is surrounded by 16 unpaired nt, including 10 residues that are >95% conserved among the known 140 tmRNA sequences. All these residues were mutated to define their putative role(s) in trans-translation. Both the extent of aminoacylation and the alanine incorporation into the tag sequence, reflecting the two functions of tmRNA, were measured in vitro for all variants. As anticipated from the low sequence conservation, mutating positions 8-12 and position 15 affects neither aminoacylation nor protein tagging. Mutating a set of two conserved positions 13 and 14 abolishes both functions. Probing the solution conformation indicates that this defective mutant adopts an alternate conformation of its acceptor stem that is no more aminoacylatable, and thus inactive in protein tagging. Selected point mutations at the conserved nucleotide stretches 16-20 and 333-335 seriously impair protein tagging with only minor changes in their solution conformations and aminoacylation. Point mutations at conserved positions 19 and 334 abolish trans-translation and 70S ribosome binding, although retaining nearly normal aminoacylation capacities. Two proteins that are known to interact with tmRNA were purified, and their interactions with the defective RNA variants were examined in vitro. Based on phylogenetic and functional data, an additional structural motif consisting of a quartet composed of non-Watson-Crick base pairs 5'-YGAC-3':5'-GGAC-3' involving some of the conserved nucleotides next to the tRNA-like portion is proposed. Overall, the highly conserved nucleotides around the tRNA-like portion are maintained for both structural and functional requirements during evolution.
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