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Correction

Correction: Salinas-Giegé et al. tRNA Biology in Mitochondria. Int. J. Mol. Sci. 2015, 16, 4518–4559

by
Thalia Salinas-Giegé
1,†,
Richard Giegé
2,† and
Philippe Giegé
1,*,†
1
Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique, Université de Strasbourg, 12 rue du Général Zimmer, F-67084 Strasbourg Cedex, France
2
Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, Université de Strasbourg, 15 rue René Descartes, F-67084 Strasbourg Cedex, France
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2026, 27(1), 367; https://doi.org/10.3390/ijms27010367 (registering DOI)
Submission received: 7 August 2025 / Accepted: 25 November 2025 / Published: 29 December 2025
(This article belongs to the Section Biochemistry)
There was an error in the original publication [1]. The sentence “Similarly, in the moss P. patens, cytosolic tRNAArg(ACG) is imported in mitochondria where it undergoes an A to I editing at the wobble position of the anticodon [193]” on Paragraph 2 of Section 4.3.2 is incorrect.
A correction has been made to Section 4 ‘Biogenesis of Functional Mitochondrial tRNAs’, Section 4.3 ‘Functions and Mechanisms for tRNA Modifications and Editing’, Section 4.3.2 ‘Mitochondrial tRNA Editing’, Paragraph 2:
Beyond the mitochondrial encoded tRNAs, editing processes were also reported for cytosolic tRNAs imported into mitochondria. For instance, it was shown in L. tarentolae that a specific C to U editing in the anticodon of the imported nonedited tRNATrp allows the decoding of mitochondrial UGA codons as tryptophans [192]. In contrast, in the moss P. patens a tRNAArg(ACG) isoacceptor encoded in mitochondria, thus not imported from the cytosol, is deaminated at position A34 to obtain an ICG anticodon [193]. Interestingly for protozoan tRNATrp, import and editing have drastic structural consequences, since this tRNA is partially thiolated at universally conserved position 33 to s2U33 and O′-methylated at the ribose moiety of Ψ32 as well as on edited U34 and nonedited C34 [194]. The presence of s2U33 and the concentration of O′-methylated pyrimidines in the anticodon domain, likely is the prerequisite for proper decoding of the Trp codon by conferring conformation rigidity and chemical stability to the anticodon loop. In contrast, dethiolation of cmm5s2U within mitochondria at wobble position 34 of imported trypanosomatid tRNAs, as explicitly shown for T. brucei tRNAGlu, is an alternate editing mechanisms required to modulate decoding [195].
The authors state that the scientific conclusions are unaffected. This correction was approved by the Academic Editor. The original publication has also been updated.

Reference

  1. Salinas-Giegé, T.; Giegé, R.; Giegé, P. tRNA Biology in Mitochondria. Int. J. Mol. Sci. 2015, 16, 4518–4559. [Google Scholar] [CrossRef] [PubMed]
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MDPI and ACS Style

Salinas-Giegé, T.; Giegé, R.; Giegé, P. Correction: Salinas-Giegé et al. tRNA Biology in Mitochondria. Int. J. Mol. Sci. 2015, 16, 4518–4559. Int. J. Mol. Sci. 2026, 27, 367. https://doi.org/10.3390/ijms27010367

AMA Style

Salinas-Giegé T, Giegé R, Giegé P. Correction: Salinas-Giegé et al. tRNA Biology in Mitochondria. Int. J. Mol. Sci. 2015, 16, 4518–4559. International Journal of Molecular Sciences. 2026; 27(1):367. https://doi.org/10.3390/ijms27010367

Chicago/Turabian Style

Salinas-Giegé, Thalia, Richard Giegé, and Philippe Giegé. 2026. "Correction: Salinas-Giegé et al. tRNA Biology in Mitochondria. Int. J. Mol. Sci. 2015, 16, 4518–4559" International Journal of Molecular Sciences 27, no. 1: 367. https://doi.org/10.3390/ijms27010367

APA Style

Salinas-Giegé, T., Giegé, R., & Giegé, P. (2026). Correction: Salinas-Giegé et al. tRNA Biology in Mitochondria. Int. J. Mol. Sci. 2015, 16, 4518–4559. International Journal of Molecular Sciences, 27(1), 367. https://doi.org/10.3390/ijms27010367

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