Structural basis of translation termination, rescue, and recycling in mammalian mitochondria

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Structural basis of translation termination, rescue, and recycling in mammalian mitochondria. / Kummer, Eva; Schubert, Katharina Noel; Schoenhut, Tanja; Scaiola, Alain; Ban, Nenad.

In: Molecular Cell, Vol. 81, No. 12, 2021, p. 2566-2582.e6.

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

Harvard

Kummer, E, Schubert, KN, Schoenhut, T, Scaiola, A & Ban, N 2021, 'Structural basis of translation termination, rescue, and recycling in mammalian mitochondria', Molecular Cell, vol. 81, no. 12, pp. 2566-2582.e6. https://doi.org/10.1016/j.molcel.2021.03.042

APA

Kummer, E., Schubert, K. N., Schoenhut, T., Scaiola, A., & Ban, N. (2021). Structural basis of translation termination, rescue, and recycling in mammalian mitochondria. Molecular Cell, 81(12), 2566-2582.e6. https://doi.org/10.1016/j.molcel.2021.03.042

Vancouver

Kummer E, Schubert KN, Schoenhut T, Scaiola A, Ban N. Structural basis of translation termination, rescue, and recycling in mammalian mitochondria. Molecular Cell. 2021;81(12):2566-2582.e6. https://doi.org/10.1016/j.molcel.2021.03.042

Author

Kummer, Eva ; Schubert, Katharina Noel ; Schoenhut, Tanja ; Scaiola, Alain ; Ban, Nenad. / Structural basis of translation termination, rescue, and recycling in mammalian mitochondria. In: Molecular Cell. 2021 ; Vol. 81, No. 12. pp. 2566-2582.e6.

Bibtex

@article{6d13a42c23194d2bbf017e899fdd4ec6,
title = "Structural basis of translation termination, rescue, and recycling in mammalian mitochondria",
abstract = "The mitochondrial translation system originates from a bacterial ancestor but has substantially diverged in the course of evolution. Here, we use single-particle cryo-electron microscopy (cryo-EM) as a screening tool to identify mitochondrial translation termination mechanisms and to describe them in molecular detail. We show how mitochondrial release factor 1a releases the nascent chain from the ribosome when it encounters the canonical stop codons UAA and UAG. Furthermore, we define how the peptidyl-tRNA hydrolase ICT1 acts as a rescue factor on mitoribosomes that have stalled on truncated messages to recover them for protein synthesis. Finally, we present structural models detailing the process of mitochondrial ribosome recycling to explain how a dedicated elongation factor, mitochondrial EFG2 (mtEFG2), has specialized for cooperation with the mitochondrial ribosome recycling factor to dissociate the mitoribosomal subunits at the end of the translation process.",
author = "Eva Kummer and Schubert, {Katharina Noel} and Tanja Schoenhut and Alain Scaiola and Nenad Ban",
note = "Copyright {\textcopyright} 2021 Elsevier Inc. All rights reserved.",
year = "2021",
doi = "10.1016/j.molcel.2021.03.042",
language = "English",
volume = "81",
pages = "2566--2582.e6",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "12",

}

RIS

TY - JOUR

T1 - Structural basis of translation termination, rescue, and recycling in mammalian mitochondria

AU - Kummer, Eva

AU - Schubert, Katharina Noel

AU - Schoenhut, Tanja

AU - Scaiola, Alain

AU - Ban, Nenad

N1 - Copyright © 2021 Elsevier Inc. All rights reserved.

PY - 2021

Y1 - 2021

N2 - The mitochondrial translation system originates from a bacterial ancestor but has substantially diverged in the course of evolution. Here, we use single-particle cryo-electron microscopy (cryo-EM) as a screening tool to identify mitochondrial translation termination mechanisms and to describe them in molecular detail. We show how mitochondrial release factor 1a releases the nascent chain from the ribosome when it encounters the canonical stop codons UAA and UAG. Furthermore, we define how the peptidyl-tRNA hydrolase ICT1 acts as a rescue factor on mitoribosomes that have stalled on truncated messages to recover them for protein synthesis. Finally, we present structural models detailing the process of mitochondrial ribosome recycling to explain how a dedicated elongation factor, mitochondrial EFG2 (mtEFG2), has specialized for cooperation with the mitochondrial ribosome recycling factor to dissociate the mitoribosomal subunits at the end of the translation process.

AB - The mitochondrial translation system originates from a bacterial ancestor but has substantially diverged in the course of evolution. Here, we use single-particle cryo-electron microscopy (cryo-EM) as a screening tool to identify mitochondrial translation termination mechanisms and to describe them in molecular detail. We show how mitochondrial release factor 1a releases the nascent chain from the ribosome when it encounters the canonical stop codons UAA and UAG. Furthermore, we define how the peptidyl-tRNA hydrolase ICT1 acts as a rescue factor on mitoribosomes that have stalled on truncated messages to recover them for protein synthesis. Finally, we present structural models detailing the process of mitochondrial ribosome recycling to explain how a dedicated elongation factor, mitochondrial EFG2 (mtEFG2), has specialized for cooperation with the mitochondrial ribosome recycling factor to dissociate the mitoribosomal subunits at the end of the translation process.

U2 - 10.1016/j.molcel.2021.03.042

DO - 10.1016/j.molcel.2021.03.042

M3 - Journal article

C2 - 33878294

VL - 81

SP - 2566-2582.e6

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 12

ER -

ID: 274230754