5′‐End sequencing in Saccharomyces cerevisiae offers new insights into 5′‐ends of tRNAHis and snoRNAs. Issue 9 (4th April 2019)

• Record Type: Journal Article
• Authors: Dodbele, Samantha; Moreland, Blythe; Gardner, Spencer M.; Bundschuh, Ralf; Jackman, Jane E.
• Is Part Of: FEBS letters. Volume 593:Issue 9(2019)
• Page Start: 971
• Page End: 981
• Publication Date: 2019-04-04
• Subjects: 3′–5′ polymerization -- Bacillus thuringiensis -- RNA‐Seq -- Saccharomyces cerevisiae -- snoRNA -- tRNAHis; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13364
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : tRNA H is guanylyltransferase (Thg1) specifies eukaryotic tRNA H is identity by catalysing a 3′–5′ non‐Watson–Crick (WC) addition of guanosine to the 5′‐end of tRNA H is . 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 :