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  Structural basis of GTPase-mediated mitochondrial ribosome biogenesis and recycling

Hillen, H. S., Lavdovskaia, E., Nadler, F., Hanitsch, E., Linden, A., Bohnsack, K. E., et al. (2021). Structural basis of GTPase-mediated mitochondrial ribosome biogenesis and recycling. Nature Communications, 12: 3672. doi:10.1038/s41467-021-23702-y.

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 Creators:
Hillen, H. S.1, Author              
Lavdovskaia, E., Author
Nadler, F., Author
Hanitsch, E., Author
Linden, A.2, Author              
Bohnsack, K. E., Author
Urlaub, H.3, Author              
Richter-Dennerlein, R., Author
Affiliations:
1Research Group Structure and Function of Molecular Machines, MPI for Biophysical Chemistry, Max Planck Society, ou_3265856              
2Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              
3Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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Free keywords: Cryoelectron microscopy; Ribosomal proteins; Ribosome; Ribozymes
 Abstract: Ribosome biogenesis requires auxiliary factors to promote folding and assembly of ribosomal proteins and RNA. Particularly, maturation of the peptidyl transferase center (PTC) is mediated by conserved GTPases, but the molecular basis is poorly understood. Here, we define the mechanism of GTPase-driven maturation of the human mitochondrial large ribosomal subunit (mtLSU) using endogenous complex purification, in vitro reconstitution and cryo-EM. Structures of transient native mtLSU assembly intermediates that accumulate in GTPBP6-deficient cells reveal how the biogenesis factors GTPBP5, MTERF4 and NSUN4 facilitate PTC folding. Addition of recombinant GTPBP6 reconstitutes late mtLSU biogenesis in vitro and shows that GTPBP6 triggers a molecular switch and progression to a near-mature PTC state. Additionally, cryo-EM analysis of GTPBP6-treated mature mitochondrial ribosomes reveals the structural basis for the dual-role of GTPBP6 in ribosome biogenesis and recycling. Together, these results provide a framework for understanding step-wise PTC folding as a critical conserved quality control checkpoint.

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Language(s): eng - English
 Dates: 2021-06-16
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-021-23702-y
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Title: Nature Communications
Source Genre: Journal
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Pages: 10 Volume / Issue: 12 Sequence Number: 3672 Start / End Page: - Identifier: -