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. 2022 Oct 28;50(20):11992. doi: 10.1093/nar/gkac1057

Correction to ‘Human Thg1 displays tRNA-inducible GTPase activity’

PMCID: PMC9723608  PMID: 36305790

Nucleic Acids Research, Volume 50, Issue 17, 23 September 2022, Pages 10015–10025, https://doi.org/10.1093/nar/gkac768

In the originally published version of this manuscript, there was an error in Figure 6: the product of GTP hydrolysis was PPi instead of Pi.

Figure 6.

Figure 6.

A possible interplay between G-1 addition and GTP hydrolysis by human Thg1. The protein structure was obtained from dimeric human Thg1-dGTP complex (PDB ID: 3OTB). Subunits A and B of human Thg1 are colored in wheat and turquoise, respectively. The adenylylation and guanylylation sites are marked as ‘A’ and ‘G’, respectively. Under conditions with a high ATP/GTP ratio, HsThg1 preferentially catalyzes G-1 incorporation into tRNAmHis (reactions 1 to 4), whereas under conditions with a low ATP/GTP ratio, HsThg1 preferentially catalyzes the hydrolysis of GTP to GDP (reactions a to b).

This error has been corrected online.


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