Hierarchical folding of the catalytic core during mitochondrial ribosome biogenesis

Lavdovskaia, Elena; Hillen, Hauke S.; Richter‐Dennerlein, Ricarda

doi:10.1016/j.tcb.2021.09.004

Cited by 15 publications

(5 citation statements)

References 16 publications

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“…Interestingly, we also identified assembly factors of respiratory chain complexes IV, such as COX20 ( Bourens et al, 2014 ; Lorenzi et al, 2018 ) or COA1 ( Wang et al, 2020 ). These findings suggest that the mitochondrial ribosome and its interacting partners could act as a platform to initiate OXPHOS assembly and that the mitochondrial ribosome remains associated with maturing complexes beyond the cotranslational assembly stages ( Richter-Dennerlein et al, 2016 ; Maiti et al, 2021 ; Ferrari et al, 2021 ; Lavdovskaia et al, 2021 ; Mick et al, 2012 ).…”

Section: Discussionmentioning

confidence: 95%

“…However, the mechanisms underlying coordination of mitochondrial translation with OXPHOS assembly and the involved factors remain poorly understood ( Richter-Dennerlein et al, 2015 ; Dennerlein et al, 2017 ; Kummer and Ban, 2021 ; Hällberg and Larsson, 2014 ). Especially, the question as to how long the mitochondrial ribosome remains associated with biogenesis intermediates of the oxidative phosphorylation system is still unaddressed ( Richter-Dennerlein et al, 2016 ; Maiti et al, 2021 ; Ferrari et al, 2021 ; Lavdovskaia et al, 2021 ).…”

Section: Discussionmentioning

confidence: 99%

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Defining the interactome of the human mitochondrial ribosome identifies SMIM4 and TMEM223 as respiratory chain assembly factors

Dennerlein

Poerschke

Oeljeklaus

et al. 2021

eLife

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Human mitochondria express a genome that encodes thirteen core subunits of the oxidative phosphorylation system (OXPHOS). These proteins insert into the inner membrane co-translationally. Therefore, mitochondrial ribosomes engage with the OXA1L-insertase and membrane-associated proteins, which support membrane insertion of translation products and early assembly steps into OXPHOS complexes. To identify ribosome-associated biogenesis factors for the OXPHOS system, we purified ribosomes and associated proteins from mitochondria. We identified TMEM223 as a ribosome-associated protein involved in complex IV biogenesis. TMEM223 stimulates the translation of COX1 mRNA and is a constituent of early COX1 assembly intermediates. Moreover, we show that SMIM4 together with C12ORF73 interacts with newly synthesized cytochrome b to support initial steps of complex III biogenesis in complex with UQCC1 and UQCC2. Our analyses define the interactome of the human mitochondrial ribosome and reveal novel assembly factors for complex III and IV biogenesis that link early assembly stages to the translation machinery.

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Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Defining the interactome of the human mitochondrial ribosome identifies SMIM4 and TMEM223 as respiratory chain assembly factors

Dennerlein

Poerschke

Oeljeklaus

et al. 2021

eLife

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“…In the resulting CP dataset, we selected a list of mitochondrial gene expression factors based on recent reviews (48)(49)(50)(51)(52) and arranged this list of 164 proteins according to their molecular functions and migration profiles (Suppl. Data 3).…”

Section: Characterization Of the High Molecular Mass Range Cluster Of...mentioning

confidence: 99%

Let’s make it clear: Systematic exploration of mitochondrial DNA- and RNA-protein complexes by complexome profiling

Potter¹,

Cabrera‐Orefice

Spelbrink³

2023

Preprint

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Complexome profiling (CP) is a powerful tool for systematic investigation of protein interactors that has been primarily applied to study the composition and dynamics of mitochondrial protein complexes. Here, we further optimised this method to extend its application to survey mitochondrial DNA- and RNA-interacting protein complexes. We established that high-resolution clear native gel electrophoresis (hrCNE) is a better alternative to preserve DNA- and RNA-protein interactions that are otherwise disrupted when samples are separated by the widely used blue native gel electrophoresis (BNE). In combination with enzymatic digestion of DNA, our CP approach improved the identification of a wide range of protein interactors of the mitochondrial gene expression system without compromising the detection of other multi-protein complexes. The utility of this approach was particularly demonstrated by analysing the complexome changes in human mitochondria with impaired gene expression after transient, chemically-induced mtDNA depletion. Effects of RNase on mitochondrial protein complexes were also evaluated and discussed. Overall, our adaptations significantly improved the identification of mitochondrial DNA- and RNA-protein interactions by CP, thereby unlocking the comprehensive analysis of a near-complete mitochondrial complexome in a single experiment.

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“…The GTPBP7 beta hairpin is additionally stabilized by the C-terminus of MALSU1 reaching over. The beta hairpin has earlier been shown to serve as an anchor point around which GTPBP7 swings from a conformation contacting the ribosomal immature PTC towards pre-RNA helices H68-71 upon binding of the methyltransferase MRM2 to the A loop 11 , 42 .…”

Section: Resultsmentioning

confidence: 99%

Structural insights into the role of GTPBP10 in the RNA maturation of the mitoribosome

Nguyen,

Ritter,

Kummer

2023

Nat Commun

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Mitochondria contain their own genetic information and a dedicated translation system to express it. The mitochondrial ribosome is assembled from mitochondrial-encoded RNA and nuclear-encoded ribosomal proteins. Assembly is coordinated in the mitochondrial matrix by biogenesis factors that transiently associate with the maturing particle. Here, we present a structural snapshot of a large mitoribosomal subunit assembly intermediate containing 7 biogenesis factors including the GTPases GTPBP7 and GTPBP10. Our structure illustrates how GTPBP10 aids the folding of the ribosomal RNA during the biogenesis process, how this process is related to bacterial ribosome biogenesis, and why mitochondria require two biogenesis factors in contrast to only one in bacteria.

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Hierarchical folding of the catalytic core during mitochondrial ribosome biogenesis

Cited by 15 publications

References 16 publications

Defining the interactome of the human mitochondrial ribosome identifies SMIM4 and TMEM223 as respiratory chain assembly factors

Defining the interactome of the human mitochondrial ribosome identifies SMIM4 and TMEM223 as respiratory chain assembly factors

Let’s make it clear: Systematic exploration of mitochondrial DNA- and RNA-protein complexes by complexome profiling

Structural insights into the role of GTPBP10 in the RNA maturation of the mitoribosome

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