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• W2079386209 abstract "The tRNA His guanylyltransferase (Thg1) family comprises a set of unique 3′–5′ nucleotide addition enzymes found ubiquitously in Eukaryotes, where they function in the critical G −1 addition reaction required for tRNA His maturation. However, in most Bacteria and Archaea, G −1 is genomically encoded; thus post-transcriptional addition of G −1 to tRNA His is not necessarily required. The presence of highly conserved Thg1-like proteins (TLPs) in more than 40 bacteria and archaea therefore suggests unappreciated roles for TLP-catalyzed 3′–5′ nucleotide addition. Here, we report that TLPs from Bacillus thuringiensis (BtTLP) and Methanosarcina acetivorans (MaTLP) display biochemical properties consistent with a prominent role in tRNA 5′-end repair. Unlike yeast Thg1, BtTLP strongly prefers addition of missing N +1 nucleotides to 5′-truncated tRNAs over analogous additions to full-length tRNA ( kcat / KM enhanced 5–160-fold). Moreover, unlike for −1 addition, BtTLP-catalyzed additions to truncated tRNAs are not biased toward addition of G, and occur with tRNAs other than tRNA His . Based on these distinct biochemical properties, we propose that rather than functioning solely in tRNA His maturation, bacterial and archaeal TLPs are well-suited to participate in tRNA quality control pathways. These data support more widespread roles for 3′–5′ nucleotide addition reactions in biology than previously expected." @default.
• W2079386209 created "2016-06-24" @default.
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• W2079386209 date "2010-11-03" @default.
• W2079386209 modified "2023-10-16" @default.
• W2079386209 title "tRNA 5′-end repair activities of tRNA His guanylyltransferase (Thg1)-like proteins from Bacteria and Archaea" @default.
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• W2079386209 doi "https://doi.org/10.1093/nar/gkq976" @default.
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