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Open Access

Correction

Correction: Archaeal Tuc1/Ncs6 Homolog Required for Wobble Uridine tRNA Thiolation Is Associated with Ubiquitin-Proteasome, Translation, and RNA Processing System Homologs

  • The PLOS ONE Staff

File S1 is corrupted and will not open. Please view the correct File S1 here.

Supporting Information

File S1.

Supporting Information. File S1 includes: Table S1. Strains, plasmids used in this study; Table S2. Oligonucleotide primers used in this study; Figure S1. Dendrogram analysis of Haloferax volcanii NcsA and homologs of the α hydrolase (ANH) superfamily from archaea, eukaryotes and bacteria; Figure S2. 3D-structural model of Haloferax volcanii NcsA; Figure S3. Organization of ncsA and its targeted deletion on the genome of Haloferax volcanii; Figure S4. Growth of Haloferax volcanii ΔncsA mutant compared to parent strain H26 at optimum growth temperature; Figure S5. Lys204 residue of NcsA is found isopeptide linked to SAMP2; Figure S6. Detection of E1-like UbaA and PAN-A/1 ATPase in NcsA-StrepII pull-down fractions.

https://doi.org/10.1371/journal.pone.0115719.s001

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Reference

  1. 1. Chavarria NE, Hwang S, Cao S, Fu X, Holman M, et al. (2014) Archaeal Tuc1/Ncs6 Homolog Required for Wobble Uridine tRNA Thiolation Is Associated with Ubiquitin-Proteasome, Translation, and RNA Processing System Homologs. PLoS ONE 9(6): e99104

Citation: The PLOS ONE Staff (2014) Correction: Archaeal Tuc1/Ncs6 Homolog Required for Wobble Uridine tRNA Thiolation Is Associated with Ubiquitin-Proteasome, Translation, and RNA Processing System Homologs. PLoS ONE 9(12): e115719. https://doi.org/10.1371/journal.pone.0115719

Published: December 16, 2014

Copyright: © 2014 The PLOS ONE Staff. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.