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  NSUN3 and ABH1 modify the wobble position of mt-tRNAMet to expand codon recognition in mitochondrial translation.

Haag, S., Sloan, K. E., Ranjan, N., Warda, A. S., Kretschmer, J., Blessing, C., et al. (2016). NSUN3 and ABH1 modify the wobble position of mt-tRNAMet to expand codon recognition in mitochondrial translation. The EMBO Journal, 35(19), 2104-2119. doi:10.15252/embj.201694885.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-2FBA-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-AE86-0
Genre: Journal Article

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 Creators:
Haag, S., Author
Sloan, K. E., Author
Ranjan, N.1, Author              
Warda, A. S., Author
Kretschmer, J., Author
Blessing, C., Author
Hübner, B., Author
Seikowski, J.2, Author              
Dennerlein, S., Author
Rehling, P.3, Author              
Rodnina, M. V.1, Author              
Höbartner, C.2, Author              
Bohnsack, M. T., Author
Affiliations:
1Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578598              
2Research Group of Nucleic Acid Chemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578605              
3Max Planck Fellow Peter Rehling, ou_1298545              

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Free keywords: ABH1; mitochondria; NSUN3; RNA modification; translation
 Abstract: Mitochondrial gene expression uses a non-universal genetic code in mammals. Besides reading the conventional AUG codon, mitochondrial (mt-)tRNAMet mediates incorporation of methionine on AUA and AUU codons during translation initiation and on AUA codons during elongation. We show that the RNA methyltransferase NSUN3 localises to mitochondria and interacts with mt-tRNAMet to methylate cytosine 34 (C34) at the wobble position. NSUN3 specifically recognises the anticodon stem loop (ASL) of the tRNA, explaining why a mutation that compromises ASL basepairing leads to disease. We further identify ALKBH1/ABH1 as the dioxygenase responsible for oxidising m5C34 of mt-tRNAMet to generate an f5C34 modification. In vitro codon recognition studies with mitochondrial translation factors reveal preferential utilisation of m5C34 mt-tRNAMet in initiation. Depletion of either NSUN3 or ABH1 strongly affects mitochondrial translation in human cells, implying that modifications generated by both enzymes are necessary for mt-tRNAMet function. Together, our data reveal how modifications in mt-tRNAMet are generated by the sequential action of NSUN3 and ABH1, allowing the single mitochondrial tRNAMet to recognise the different codons encoding methionine.

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Language(s): eng - English
 Dates: 2016-08-062016-10-04
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.15252/embj.201694885
 Degree: -

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Title: The EMBO Journal
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 35 (19) Sequence Number: - Start / End Page: 2104 - 2119 Identifier: -