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Extra resources for Anisotropic diffusion
G. via protein–protein interaction motifs in the C-terminal domain and, in this way, contribute substrate specificity of the T. brucei ligases. Two 3′-terminal uridylyl transferases (TUTases) have been identified in T. brucei, one of which is part of the editosome complexes (Ernst et al. 2003). This enzyme, named TbMP57, primarily adds a single U to the 3′ end of ssRNA, with a preference for a 3′-terminal A or G. It also adds the specified number of Us to a pre-cleaved double-stranded RNA editing substrate, reflecting the characteristics of natural insertion editing events (Ernst et al.
Scientist at the time were amidst trying to explain how (or why) 20 different amino acids required 61 different codons for protein synthesis. The discovery of inosine in yeast tRNAAla (AUA) (because of its predicted base-pairing properties) led Crick to propose that the base-pair capabilities of this tRNA were not limited to the four canonical nucleotides. Crick reasoned that the newly discovered, inosine-containing tRNAAla (AUA) could pair with three different codons (ending in A, C, or U) to specify the same amino acid.
Eur J Biochem 270:4070–4081 30 M. Homann Nelson JA, Uhlenbeck OC (2006) When to believe what you see. Mol Cell 23:447–450 Noller HF (2005) RNA structure: reading the ribosome. Science 309:1508–1514 Öhman M, Kallman AM, Bass BL (2000) In vitro analysis of the binding of ADAR2 to the premRNA encoding the GluR-B R/G site. RNA 6:687–697 Palazzo SS, Panigrahi AK, Igo RP, Salavati R, Stuart K (2003) Kinetoplastid RNA editing ligases: complex association, characterization, and substrate requirements. Mol Biochem Parasitol 127:161–167 Panigrahi AK, Schnaufer A, Ernst NL, Wang B, Carmean N, Salavati R, Stuart K (2003) Identification of novel components of Trypanosoma brucei editosomes.