Researchers are exploring whether these ubiquitous fluorinated molecules might worsen infections or hamper vaccine effectiveness.
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BIOCHEMISTRY Correction for “Mod5 protein binds to tRNA gene complexes and affects local transcriptional silencing,” by Matthew Pratt-Hyatt, Dave A. Pai, Rebecca A. Haeusler, Glenn G. Wozniak, Paul D. Good, Erin L. Miller, Ian X. McLeod, John R. Yates III, Anita K. Hopper, and David R. Engelke, which appeared in issue 33, August 13, 2013, of Proc Natl Acad Sci USA (110:E3081–E3089; first published July 29, 2013;10.1073/pnas.1219946110).
The authors note that Fig. 5 appeared incorrectly. The corrected figure and its legend appear below.
Fig. 5.
Conservation of the Mod5 protein and silencing function in eukaryotes. (A) The alignment of three Mod5 proteins from S. cerevisiae, A. thaliana, and H. sapiens is depicted, with areas of conservation indicated by shaded boxes. All variants contain motifs for ATP/GTP binding and DMAPP binding, including E. coli (14, 40). Eukaryotic homologs also have a zinc finger motif in the C-terminal extensions. (B) tgm silencing functions of yeast Mod5 are conserved in plant and human proteins. It was previously shown that human and Arabidopsis Mod5 homologs are able to restore i6A modification of tRNAs in yeast in an mod5∆ strain (14, 24). Plasmids expressing these ORFs were tested for supporting tgm silencing in an mod5∆ strain containing a tgm silencing reporter plasmid, with loss of silencing shown by growth on media lacking histidine (−His). Although both homologs restore silencing, the H. sapiens version of Mod5 (TRIT1) is consistently more robust in preventing growth without histidine.
Correction for Pratt-Hyatt et al., Mod5 protein binds to tRNA gene complexes and affects local transcriptional silencing
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