RT Journal Article
SR Electronic
T1 <em>Arabidopsis</em> TRM5 encodes a nuclear-localised bifunctional tRNA guanine and inosine-N1-methyltransferase that is important for growth
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 485516
DO 10.1101/485516
A1 Q. Guo
A1 PQ. Ng
A1 S. Shi
A1 D. Fan
A1 J. Li
A1 H. Wang
A1 T. Do
A1 R. David
A1 P. Mittal
A1 R. Bock
A1 M. Zhao
A1 W. Zhou
A1 I. R. Searle
YR 2018
UL http://biorxiv.org/content/early/2018/12/03/485516.abstract
AB Modified nucleosides in tRNAs are critical for protein translation. N1-methylguanosine-37 and N1-methylinosine-37 in tRNAs, both located at the 3’-adjacent to the anticodon, are formed by Trm5 and here we describe Arabidopsis thaliana AtTrm5 (At3g56120) as a Trm5 ortholog. We show that AtTrm5 complements the yeast trm5 mutant, and in vitro methylates tRNA guanosine-37 to produce N1-methylguanosine (m1G). We also show in vitro that AtTRM5 methylates tRNA inosine-37 to produce N1-methylinosine (m1I) and in Attrm5 mutant plants, we show a reduction of both N1-methylguanosine and N1-methylinosine. We also show that AtTRM5 is localized to the nucleus in plant cells. Attrm5 mutant plants have overall slower growth as observed by slower leaf initiation rate, delayed flowering and reduced primary root length. In Attrm5 mutants, mRNAs of flowering time genes are less abundant and correlated with delayed flowering. Finally, proteomics data show that photosynthetic protein abundance is affected in mutant plants. Our findings highlight the bifunctionality of AtTRM5 and the importance of the post-transcriptional tRNA modifications m1G and m1I at tRNA position 37 in general plant growth and development.