3'-5' tRNAHis guanylyltransferase in bacteria.

FEBS Letters
Ilka U HeinemannDieter Söll

Abstract

The identity of the histidine specific transfer RNA (tRNA(His)) is largely determined by a unique guanosine residue at position -1. In eukaryotes and archaea, the tRNA(His) guanylyltransferase (Thg1) catalyzes 3'-5' addition of G to the 5'-terminus of tRNA(His). Here, we show that Thg1 also occurs in bacteria. We demonstrate in vitro Thg1 activity for recombinant enzymes from the two bacteria Bacillus thuringiensis and Myxococcus xanthus and provide a closer investigation of several archaeal Thg1. The reaction mechanism of prokaryotic Thg1 differs from eukaryotic enzymes, as it does not require ATP. Complementation of a yeast thg1 knockout strain with bacterial Thg1 verified in vivo activity and suggests a relaxed recognition of the discriminator base in bacteria.

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Citations

Nov 17, 2010·Proceedings of the National Academy of Sciences of the United States of America·John J Perona, Javin P Oza
Sep 6, 2011·Nucleic Acids Research·Ilka U HeinemannDieter Söll
Dec 18, 2012·Nucleic Acids Research·Bhalchandra S RaoJane E Jackman
Mar 30, 2012·RNA·Jane E JackmanMichael W Gray
Dec 11, 2013·Proceedings of the National Academy of Sciences of the United States of America·Akiyoshi NakamuraMin Yao
Dec 24, 2014·International Journal of Molecular Sciences·Heike BetatMario Mörl
May 11, 2015·Nucleic Acids Research·Sandra WendeMario Mörl
Aug 4, 2016·Nucleic Acids Research·Yicheng LongJane E Jackman
Jun 20, 2012·Biochemistry·Michael W Gray
Oct 30, 2016·RNA Biology·Christiane Rammelt, Walter Rossmanith
Jun 18, 2017·Biochemical and Biophysical Research Communications·Kitaik LeeKwang Yeon Hwang
Apr 17, 2014·The Journal of Biological Chemistry·Maria G AbadJane E Jackman
May 22, 2021·Royal Society Open Science·Jana WiedermannováYulia Yuzenkova

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