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Short lines indicate Watson-Crick pairings (G-C and A-U) dots are G-U pairings. Shown are the 5' and 3' ends of the 363-nucleotide RNA chain numbered in increments of ten. Structure Secondary structure of the standard one-piece tmRNAs It also revealed differences from tRNA: the anticodon arm is missing in tmRNA, and the D arm region is a loop without base pairs.
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Subsequent sequence comparison revealed the full tRNA-like domain (TLD) formed by the 5' and 3' ends of tmRNA, including the acceptor stem with elements like those in alanine tRNA that promote its aminoacylation by alanine-tRNA ligase. The similarity at the 3' end of tmRNA to the T stem-loop of tRNA was first recognized upon sequencing ssrA from Mycobacterium tuberculosis. The presence of pseudouridine in the mixed 10S RNA hinted that tmRNA has modified bases found also in tRNA.
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TmRNA was first designated 10Sa RNA after a mixed "10S" electrophoretic fraction of Escherichia coli RNA was further resolved into tmRNA and the similarly-sized RNase P RNA (10Sb).
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The tmRNA is remarkably versatile: it recycles the stalled ribosome, adds a proteolysis-inducing tag to the unfinished polypeptide, and facilitates the degradation of the aberrant messenger RNA. In trans-translation, tmRNA and its associated proteins bind to bacterial ribosomes which have stalled in the middle of protein biosynthesis, for example when reaching the end of a messenger RNA which has lost its stop codon. The tmRNA forms a ribonucleoprotein complex ( tmRNP) together with Small Protein B ( SmpB), Elongation Factor Tu ( EF-Tu), and ribosomal protein S1. Transfer-messenger RNA (abbreviated tmRNA, also known as 10Sa RNA and by its genetic name SsrA) is a bacterial RNA molecule with dual tRNA-like and messenger RNA-like properties.