Fig. 1: D modifications at positions 16 and 17 of human cytoplasmic tRNAs. | Communications Biology

Fig. 1: D modifications at positions 16 and 17 of human cytoplasmic tRNAs.

From: Human DUS1L catalyzes dihydrouridine modification at tRNA positions 16/17, and DUS1L overexpression perturbs translation

Fig. 1

a Chemical structure of D. b Secondary structure of human cytoplasmic tRNATyr(GUA) with modified nucleosides: 2-methylguanosine (m2G), 3-(3-amino-3-carboxypropyl)uridine (acp3U), N2,N2-dimethylguanosine (m22G), galactosyl-queuosine (galQ), pseudouridine (Ψ), N1-methylguanosine (m1G), 2’-O-methylpseudouridine (Ψm), 7-methylguanosine (m7G), 5-methylcytidine (m5C), 5-methyluridine (m5U), and N1-methyladenosine (m1A). Nucleoside positions are numbered following conventional guidelines61. Modified nucleosides are depicted according to a previous study60. c Neighbor-joining tree of DUS homologs from E. coli, S. cerevisiae, and H. sapiens generated by alignment of protein sequences and depiction of a cladogram using Clustal omega62 and its associated applications. The DUS homologs and their RefSeq numbers are as follows: E. coli DusA (NP_418473.3), DusB (NP_417726.1), and DusC (NP_416645.1); S. cerevisiae Dus1p (NP_013631.1), Dus2p (NP_014412.1), Dus3p (NP_013505.4), and Dus4p (NP_013509.1); and H. sapiens DUS1L (NP_071439.3), DUS2L (NP_001258691.1), DUS3L (NP_064560.2), and DUS4L (NP_853559.1).

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