Nature, volume 606, issue 7914, pages 603-608

Mechanism of mitoribosomal small subunit biogenesis and preinitiation

Yuzuru Itoh ¹

Anas Khawaja ^{2, 3}

Ivan G. Laptev ^{4, 5, 6}

Miriam Cipullo ^{2, 3}

Ilian Atanassov ⁷

Petr V. Sergiev ^{4, 5, 6, 8}

Joanna Rorbach ^{2, 3}

Alexey Amunts ¹

Hide authors affiliations Show authors affiliations: 8 affiliations

Science for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, Solna, Sweden |

Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden |

Max Planck Institute for Biology of Ageing-Karolinska Institutet Laboratory, Karolinska Institutet, Stockholm, Sweden |

⁴

Center of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia |

⁵

Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia |

⁶

Belozersky Institute of Physico-chemical Biology, Lomonosov Moscow State University, Moscow, Russia |

⁷

Proteomics Core Facility, Max-Planck-Institute for Biology of Ageing, Cologne, Germany |

⁸

Institute of Functional Genomics, Lomonosov Moscow State University, Moscow, Russia |

Publication type: Journal Article

Publication date: 2022-06-08

Springer Nature

Journal: Nature

Quartile SCImago

Quartile WOS

Impact factor: 64.8

ISSN: 00280836, 14764687

DOI: 10.1038/s41586-022-04795-x

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PubMed ID: 35676484

Multidisciplinary

Abstract

Mitoribosomes are essential for the synthesis and maintenance of bioenergetic proteins. Here we use cryo-electron microscopy to determine a series of the small mitoribosomal subunit (SSU) intermediates in complex with auxiliary factors, revealing a sequential assembly mechanism. The methyltransferase TFB1M binds to partially unfolded rRNA h45 that is promoted by RBFA, while the mRNA channel is blocked. This enables binding of METTL15 that promotes further rRNA maturation and a large conformational change of RBFA. The new conformation allows initiation factor mtIF3 to already occupy the subunit interface during the assembly. Finally, the mitochondria-specific ribosomal protein mS37 (ref. ¹) outcompetes RBFA to complete the assembly with the SSU–mS37–mtIF3 complex² that proceeds towards mtIF2 binding and translation initiation. Our results explain how the action of step-specific factors modulate the dynamic assembly of the SSU, and adaptation of a unique protein, mS37, links the assembly to initiation to establish the catalytic human mitoribosome.

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Itoh Y. et al. Mechanism of mitoribosomal small subunit biogenesis and preinitiation // Nature. 2022. Vol. 606. No. 7914. pp. 603-608.

GOST all authors (up to 50) Copy

Itoh Y., Khawaja A., Laptev I. G., Cipullo M., Atanassov I., Sergiev P. V., Rorbach J., Amunts A. Mechanism of mitoribosomal small subunit biogenesis and preinitiation // Nature. 2022. Vol. 606. No. 7914. pp. 603-608.

RIS |

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RIS Copy

TY - JOUR

DO - 10.1038/s41586-022-04795-x

UR - https://www.nature.com/articles/s41586-022-04795-x

TI - Mechanism of mitoribosomal small subunit biogenesis and preinitiation

T2 - Nature

AU - Itoh, Yuzuru

AU - Khawaja, Anas

AU - Laptev, Ivan G.

AU - Cipullo, Miriam

AU - Atanassov, Ilian

AU - Sergiev, Petr V.

AU - Rorbach, Joanna

AU - Amunts, Alexey

PY - 2022

DA - 2022/06/08

PB - Springer Nature

SP - 603-608

IS - 7914

VL - 606

PMID - 35676484

SN - 0028-0836

SN - 1476-4687

ER -

BibTex |

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BibTex Copy

@article{2022_Itoh,

author = {Yuzuru Itoh and Anas Khawaja and Ivan G. Laptev and Miriam Cipullo and Ilian Atanassov and Petr V. Sergiev and Joanna Rorbach and Alexey Amunts},

title = {Mechanism of mitoribosomal small subunit biogenesis and preinitiation},

journal = {Nature},

year = {2022},

volume = {606},

publisher = {Springer Nature},

month = {jun},

url = {https://www.nature.com/articles/s41586-022-04795-x},

number = {7914},

pages = {603--608},

doi = {10.1038/s41586-022-04795-x}

}

MLA

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MLA Copy

Itoh, Yuzuru, et al. “Mechanism of mitoribosomal small subunit biogenesis and preinitiation.” Nature, vol. 606, no. 7914, Jun. 2022, pp. 603-608. https://www.nature.com/articles/s41586-022-04795-x.

Found error?

Publisher

Springer Nature

Journal

Nature

Quartile SCImago

Quartile WOS

Impact factor

64.8

ISSN

00280836 (Print)
14764687 (Electronic)

Labs

Laboratory of Nucleoprotein Chemistry, Department of Chemistry of Natural Compounds, Faculty of Chemistry

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