Mouse Trmt2B protein is a dual specific mitochondrial metyltransferase responsible for m5U formation in both tRNA and rRNA
I Laptev, E Shvetsova, S Levitskii, M Serebryakova… - RNA biology, 2020 - Taylor & Francis
RNA biology, 2020•Taylor & Francis
ABSTRACT RNA molecules of all species contain modified nucleotides and particularly
m5U residues. The vertebrate mitochondrial small subunit rRNA contains m5U nucleotide in
a unique site. In this work we found an enzyme, TRMT2B, responsible for the formation of
this nucleotide and m5U residues in a number of mitochondrial tRNA species. Inactivation of
the Trmt2B gene leads to a reduction of the activity of respiratory chain complexes I, III and
IV, containing the subunits synthesized by the mitochondrial protein synthesis apparatus …
m5U residues. The vertebrate mitochondrial small subunit rRNA contains m5U nucleotide in
a unique site. In this work we found an enzyme, TRMT2B, responsible for the formation of
this nucleotide and m5U residues in a number of mitochondrial tRNA species. Inactivation of
the Trmt2B gene leads to a reduction of the activity of respiratory chain complexes I, III and
IV, containing the subunits synthesized by the mitochondrial protein synthesis apparatus …
Abstract
RNA molecules of all species contain modified nucleotides and particularly m5U residues. The vertebrate mitochondrial small subunit rRNA contains m5U nucleotide in a unique site. In this work we found an enzyme, TRMT2B, responsible for the formation of this nucleotide and m5U residues in a number of mitochondrial tRNA species. Inactivation of the Trmt2B gene leads to a reduction of the activity of respiratory chain complexes I, III and IV, containing the subunits synthesized by the mitochondrial protein synthesis apparatus. Comparative sequence analysis of m5U-specific RNA methyltransferases revealed an unusual evolutionary pathway of TRMT2B formation which includes consecutive substrate specificity switches from the large subunit rRNA to tRNA and then to the small subunit rRNA.
Taylor & Francis Online以上显示的是最相近的搜索结果。 查看全部搜索结果