A novel splice variant of Elp3/Kat9 regulates mitochondrial tRNA modification and function

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

A novel splice variant of Elp3/Kat9 regulates mitochondrial tRNA modification and function. / Boutoual, Rachid; Jo, Hyunsun; Heckenbach, Indra; Tiwari, Ritesh; Kasler, Herbert; Lerner, Chad A.; Shah, Samah; Schilling, Birgit; Calvanese, Vincenzo; Rardin, Matthew J.; Scheibye-Knudsen, Morten; Verdin, Eric.

In: Scientific Reports, Vol. 12, 14804, 2022.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Boutoual, R, Jo, H, Heckenbach, I, Tiwari, R, Kasler, H, Lerner, CA, Shah, S, Schilling, B, Calvanese, V, Rardin, MJ, Scheibye-Knudsen, M & Verdin, E 2022, 'A novel splice variant of Elp3/Kat9 regulates mitochondrial tRNA modification and function', Scientific Reports, vol. 12, 14804. https://doi.org/10.1038/s41598-022-18114-x

APA

Boutoual, R., Jo, H., Heckenbach, I., Tiwari, R., Kasler, H., Lerner, C. A., Shah, S., Schilling, B., Calvanese, V., Rardin, M. J., Scheibye-Knudsen, M., & Verdin, E. (2022). A novel splice variant of Elp3/Kat9 regulates mitochondrial tRNA modification and function. Scientific Reports, 12, [14804]. https://doi.org/10.1038/s41598-022-18114-x

Vancouver

Boutoual R, Jo H, Heckenbach I, Tiwari R, Kasler H, Lerner CA et al. A novel splice variant of Elp3/Kat9 regulates mitochondrial tRNA modification and function. Scientific Reports. 2022;12. 14804. https://doi.org/10.1038/s41598-022-18114-x

Author

Boutoual, Rachid ; Jo, Hyunsun ; Heckenbach, Indra ; Tiwari, Ritesh ; Kasler, Herbert ; Lerner, Chad A. ; Shah, Samah ; Schilling, Birgit ; Calvanese, Vincenzo ; Rardin, Matthew J. ; Scheibye-Knudsen, Morten ; Verdin, Eric. / A novel splice variant of Elp3/Kat9 regulates mitochondrial tRNA modification and function. In: Scientific Reports. 2022 ; Vol. 12.

Bibtex

@article{f342472aaa3242a29cc339c477223b14,

title = "A novel splice variant of Elp3/Kat9 regulates mitochondrial tRNA modification and function",

abstract = "Post-translational modifications, such as lysine acetylation, regulate the activity of diverse proteins across many cellular compartments. Protein deacetylation in mitochondria is catalyzed by the enzymatic activity of the NAD+-dependent deacetylase sirtuin 3 (SIRT3), however it remains unclear whether corresponding mitochondrial acetyltransferases exist. We used a bioinformatics approach to search for mitochondrial proteins with an acetyltransferase catalytic domain, and identified a novel splice variant of ELP3 (mt-ELP3) of the elongator complex, which localizes to the mitochondrial matrix in mammalian cells. Unexpectedly, mt-ELP3 does not mediate mitochondrial protein acetylation but instead induces a post-transcriptional modification of mitochondrial-transfer RNAs (mt-tRNAs). Overexpression of mt-ELP3 leads to the protection of mt-tRNAs against the tRNA-specific RNase angiogenin, increases mitochondrial translation, and furthermore increases expression of OXPHOS complexes. This study thus identifies mt-ELP3 as a non-canonical mt-tRNA modifying enzyme.",

author = "Rachid Boutoual and Hyunsun Jo and Indra Heckenbach and Ritesh Tiwari and Herbert Kasler and Lerner, {Chad A.} and Samah Shah and Birgit Schilling and Vincenzo Calvanese and Rardin, {Matthew J.} and Morten Scheibye-Knudsen and Eric Verdin",

note = "Publisher Copyright: {\textcopyright} 2022. The Author(s).",

year = "2022",

doi = "10.1038/s41598-022-18114-x",

language = "English",

volume = "12",

journal = "Scientific Reports",

issn = "2045-2322",

publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - A novel splice variant of Elp3/Kat9 regulates mitochondrial tRNA modification and function

AU - Boutoual, Rachid

AU - Jo, Hyunsun

AU - Heckenbach, Indra

AU - Tiwari, Ritesh

AU - Kasler, Herbert

AU - Lerner, Chad A.

AU - Shah, Samah

AU - Schilling, Birgit

AU - Calvanese, Vincenzo

AU - Rardin, Matthew J.

AU - Scheibye-Knudsen, Morten

AU - Verdin, Eric

PY - 2022

Y1 - 2022

N2 - Post-translational modifications, such as lysine acetylation, regulate the activity of diverse proteins across many cellular compartments. Protein deacetylation in mitochondria is catalyzed by the enzymatic activity of the NAD+-dependent deacetylase sirtuin 3 (SIRT3), however it remains unclear whether corresponding mitochondrial acetyltransferases exist. We used a bioinformatics approach to search for mitochondrial proteins with an acetyltransferase catalytic domain, and identified a novel splice variant of ELP3 (mt-ELP3) of the elongator complex, which localizes to the mitochondrial matrix in mammalian cells. Unexpectedly, mt-ELP3 does not mediate mitochondrial protein acetylation but instead induces a post-transcriptional modification of mitochondrial-transfer RNAs (mt-tRNAs). Overexpression of mt-ELP3 leads to the protection of mt-tRNAs against the tRNA-specific RNase angiogenin, increases mitochondrial translation, and furthermore increases expression of OXPHOS complexes. This study thus identifies mt-ELP3 as a non-canonical mt-tRNA modifying enzyme.

AB - Post-translational modifications, such as lysine acetylation, regulate the activity of diverse proteins across many cellular compartments. Protein deacetylation in mitochondria is catalyzed by the enzymatic activity of the NAD+-dependent deacetylase sirtuin 3 (SIRT3), however it remains unclear whether corresponding mitochondrial acetyltransferases exist. We used a bioinformatics approach to search for mitochondrial proteins with an acetyltransferase catalytic domain, and identified a novel splice variant of ELP3 (mt-ELP3) of the elongator complex, which localizes to the mitochondrial matrix in mammalian cells. Unexpectedly, mt-ELP3 does not mediate mitochondrial protein acetylation but instead induces a post-transcriptional modification of mitochondrial-transfer RNAs (mt-tRNAs). Overexpression of mt-ELP3 leads to the protection of mt-tRNAs against the tRNA-specific RNase angiogenin, increases mitochondrial translation, and furthermore increases expression of OXPHOS complexes. This study thus identifies mt-ELP3 as a non-canonical mt-tRNA modifying enzyme.

U2 - 10.1038/s41598-022-18114-x

DO - 10.1038/s41598-022-18114-x

M3 - Journal article

C2 - 36045139

AN - SCOPUS:85137042599

VL - 12

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 14804

ER -

ID: 319398455

Center for Healthy Aging