| Autor: |
Dodbele, Samantha, Moreland, Blythe, Gardner, Spencer M., Bundschuh, Ralf, Jackman, Jane E. |
| Předmět: |
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| Zdroj: |
FEBS Letters; May2019, Vol. 593 Issue 9, p971-981, 11p |
| Abstrakt: |
tRNAHis guanylyltransferase (Thg1) specifies eukaryotic tRNAHis identity by catalysing a 3′–5′ non‐Watson–Crick (WC) addition of guanosine to the 5′‐end of tRNAHis. Thg1 family enzymes in Archaea and Bacteria, called Thg1‐like proteins (TLPs), catalyse a similar but distinct 3′–5′ addition in an exclusively WC‐dependent manner. Here, a genetic system in Saccharomyces cerevisiae was employed to further assess the biochemical differences between Thg1 and TLPs. Utilizing a novel 5′‐end sequencing pipeline, we find that a Bacillus thuringiensis TLP sustains the growth of a thg1Δ strain by maintaining a WC‐dependent addition of U−1 across from A73. Additionally, we observe 5′‐end heterogeneity in S. cerevisiae small nucleolar RNAs (snoRNAs), an observation that may inform methods of annotation and mechanisms of snoRNA processing. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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