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5′‐End sequencing in Saccharomyces cerevisiae offers new insights into 5′‐ends of tRNA H is and snoRNAs
Author(s) -
Dodbele Samantha,
Moreland Blythe,
Gardner Spencer M.,
Bundschuh Ralf,
Jackman Jane E.
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13364
Subject(s) - transfer rna , saccharomyces cerevisiae , rna , biology , archaea , genetics , pseudouridine , biochemistry , ribosomal rna , guanosine , small nucleolar rna , computational biology , yeast , gene , non coding rna
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 ( TLP s), 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 TLP s. 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 A 73 . Additionally, we observe 5′‐end heterogeneity in S. cerevisiae small nucleolar RNA s (sno RNA s), an observation that may inform methods of annotation and mechanisms of sno RNA processing.