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  The human Obg protein GTPBP10 is involved in mitoribosomal biogenesis.

Lavdovskaia, E., Kolander, E., Steube, E., Mai, M. M., Urlaub, H., & Richter-Dennerlein, R. (2018). The human Obg protein GTPBP10 is involved in mitoribosomal biogenesis. Nucleic Acids Research, 46(16), 8471-8482. doi:10.1093/nar/gky701.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-E7D0-F Version Permalink: http://hdl.handle.net/21.11116/0000-0003-8649-4
Genre: Journal Article

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Lavdovskaia, E., Author
Kolander, E., Author
Steube, E., Author
Mai, M. M., Author
Urlaub, H.1, Author              
Richter-Dennerlein, R., Author
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1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: The human mitochondrial translation apparatus, which synthesizes the core subunits of the oxidative phosphorylation system, is of central interest as mutations in several genes encoding for mitoribosomal proteins or translation factors cause severe human diseases. Little is known, how this complex machinery assembles from nuclear-encoded protein components and mitochondrial-encoded RNAs, and which ancillary factors are required to form a functional mitoribosome. We have characterized the human Obg protein GTPBP10, which associates specifically with the mitoribosomal large subunit at a late maturation state. Defining its interactome, we have shown that GTPBP10 is in a complex with other mtLSU biogenesis factors including mitochondrial RNA granule components, the 16S rRNA module and late mtLSU assembly factors such as MALSU1, SMCR7L, MTERF4 and NSUN4. GTPBP10 deficiency leads to a drastic reduction in 55S monosome formation resulting in defective mtDNA-expression and in a decrease in cell growth. Our results suggest that GTPBP10 is a ribosome biogenesis factor of the mtLSU required for late stages of maturation.

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Language(s): eng - English
 Dates: 2018-08-022018-09-19
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1093/nar/gky701
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Title: Nucleic Acids Research
Source Genre: Journal
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Pages: - Volume / Issue: 46 (16) Sequence Number: - Start / End Page: 8471 - 8482 Identifier: -