The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target is correctly identified as Drosophila melanogaster Mrm2, ORF CG11447 (FlyBase FBgn0038737), encoding the protein called dmMRM2/DmMRM2. This is not the human MRM2/FTSJ2 protein or bacterial RlmE, although those orthologues provide important mechanistic evidence. The identity is confirmed by the primary fly study, which explicitly designates CG11447 as the Drosophila MRM2 orthologue. Its reported SAM-dependent RNA-methyltransferase character agrees with the supplied FtsJ/PF01728, RNA_MeTrfase_FtsJ, and class-I-like SAM-binding domain annotations (rebeloguiomar2022alatestageassembly pages 5-7, rebeloguiomar2022alatestageassembly pages 7-8).
The most defensible functional annotation is: a nuclear-encoded mitochondrial precursor that functions as a conserved FtsJ-family, SAM-dependent mitochondrial large-subunit rRNA uridine 2′-O-methyltransferase and, probably more importantly, a late mitochondrial large-ribosomal-subunit assembly factor. Direct Drosophila evidence establishes that dmMRM2 is required for mitochondrial-function-dependent development and neuronal and muscular homeostasis. However, the exact modified nucleotide, purified-enzyme activity, and assembly mechanism have not been demonstrated directly for Q9VDT6; those details are inferred from conserved human, yeast, and bacterial orthologues.
| Annotation question | Best-supported conclusion | Evidence type/species | Confidence / limitation |
|---|---|---|---|
| Identity | Target is Drosophila melanogaster Mrm2, ORF CG11447 (FlyBase FBgn0038737), protein Q9VDT6, explicitly termed DmMRM2/dmMRM2 in the primary study. | Direct nomenclature in D. melanogaster experiments (rebeloguiomar2022alatestageassembly pages 7-8) | High. Correct organism and gene; human MRM2/FTSJ2 and bacterial RlmE are orthologues, not the target. |
| Localization | Q9VDT6 is a nuclear-encoded mitochondrial precursor expected to be imported into the mitochondrial matrix, where mt-rRNA maturation and mitoribosome assembly occur, probably in or near mitochondrial RNA granules. | Supplied UniProt annotation; conserved mitochondrial pathway and human cellular context (rebeloguiomar2022alatestageassembly pages 1-2) | Moderate–high. Mitochondrial function is strongly supported, but precise sub-mitochondrial localization of endogenous fly Q9VDT6 has not been demonstrated directly. |
| Protein family and fold | dmMRM2 belongs to the FtsJ/RrmJ family of class-I-like SAM-dependent RNA methyltransferases, consistent with its RNA_MeTrfase_FtsJ/PF01728 and SAM-dependent methyltransferase-superfamily domains. | Sequence/domain annotation plus conserved MRM2 structure–function evidence (rebeloguiomar2022alatestageassembly pages 5-7) | High for family assignment; moderate for fly catalytic properties. No published structure or purified-enzyme assay of Q9VDT6 itself was identified. |
| Catalytic reaction | Predicted reaction: SAM + uridine in mitochondrial large-subunit rRNA → S-adenosyl-L-homocysteine + 2′-O-methyluridine (Um) in mt-rRNA. | Orthology and domain-based inference from human MRM2 and bacterial/yeast homologues (rebeloguiomar2022alatestageassembly pages 5-7, rorbach2014mrm2andmrm3 pages 1-2) | High-confidence inference, but not directly demonstrated using purified dmMRM2. The broad EC designation 2.1.1.- is therefore appropriate. |
| Substrate and site specificity | Predicted substrate is the mitochondrial large-subunit rRNA A-loop/H92 uridine homologous to human 16S mt-rRNA U3039, a conserved peptidyl-transferase-center position; human MRM2 installs Um3039. | Direct human RNA mapping and conserved-ribosome orthology (rebeloguiomar2022alatestageassembly pages 8-9, rebeloguiomar2022alatestageassembly pages 7-8) | Moderate–high inference for the fly orthologue. The exact Drosophila nucleotide has not been mapped experimentally; human U3039 should not be reported as the literal fly coordinate. |
| Primary biochemical role | The strongest mechanistic model is that MRM2 is a late mitochondrial large-subunit (mtLSU) assembly factor whose physical presence promotes folding/remodelling of H92, H91 and H89, maturation of the bL36m pocket, and release from an anti-association checkpoint. | Direct human knockout, catalytic rescue and 2.6-Å cryo-EM analysis of five intermediates (rebeloguiomar2022alatestageassembly pages 1-2, rebeloguiomar2022alatestageassembly pages 5-7, rebeloguiomar2022alatestageassembly pages 8-9) | High for human MRM2; strong orthology-based inference for dmMRM2. Equivalent fly assembly intermediates have not been structurally characterized. |
| Catalysis versus assembly | MRM2’s essential contribution is probably not simply production of Um: catalytically inactive human K59A and D154A variants restored mitochondrial translation without restoring U3039 methylation. | Direct human genetic complementation and LC–MS² (rebeloguiomar2022alatestageassembly pages 5-7, rebeloguiomar2022alatestageassembly pages 7-8) | High mechanistic evidence in human cells; untested directly in flies. A catalytically inactive dmMRM2 rescue experiment is needed. |
| Developmental requirement | Ubiquitous dmMRM2 RNAi caused developmental delay; few larvae pupated, most pupae died late, and rare adults were weak and malformed. Knockdown was also lethal with a second ubiquitous driver. | Direct D. melanogaster RNAi; transcript reduction measured from n=3 control and n=4 knockdown biological data points, P=0.0019 (rebeloguiomar2022alatestageassembly pages 7-8) | High phenotypic evidence. RNAi establishes requirement but is not a null allele; rescue and independent loss-of-function alleles would strengthen specificity. |
| Neuronal and muscular requirement | Pan-neuronal knockdown was lethal. Muscle-specific knockdown permitted adulthood but severely impaired startle-induced climbing, indicating a neuromuscular requirement. | Direct fly tissue-specific RNAi; climbing assay n=70 controls, n=56 knockdown, P<0.00001 (rebeloguiomar2022alatestageassembly pages 7-8) | High for tissue-level phenotypes. The assay does not distinguish primary muscle bioenergetic failure from secondary neuromuscular effects. |
| Downstream pathway | dmMRM2 acts upstream of mitoribosome biogenesis → mitochondrial translation → assembly/function of respiratory-chain OXPHOS complexes → respiration and organismal energy homeostasis. During late pupation, knockdown animals failed to show the normal increase in respiratory-chain subunits and arrested as reliance on OXPHOS increased. | Direct fly developmental immunoblot/phenotype correlation; mechanistic support from human MRM2 loss (rebeloguiomar2022alatestageassembly pages 7-8, rebeloguiomar2022alatestageassembly pages 8-9) | High for pathway placement; moderate for the precise causal chain in flies. Mitochondrial translation was not directly quantified in the reported fly experiments. |
| Quantitative orthologue context | Human MRM2 knockout reduced mean mitoribosome occupancy on mitochondrial mRNAs to 13.9% ± 7.6%; complexes I and III fell below 30% of control activity and complex IV was nearly absent. In controls, approximately 70% of mtLSU 16S rRNA carried Um3039/Gm3040 and approximately 30% retained U3039/Gm3040. | Direct human cellular measurements (rebeloguiomar2022alatestageassembly pages 2-3, rebeloguiomar2022alatestageassembly pages 7-8) | Context only—not fly statistics. These values support the conserved functional model but must not be assigned directly to Q9VDT6. |
| Recent evidence and remaining gaps | No direct 2023–2024 experimental study specific to Q9VDT6/dmMRM2 was identified. Recent human structures reinforce the conserved importance of U3039/G3040-region maturation and associated GTPases, but do not replace fly-specific validation. | 2023 human mtLSU assembly structure and 2024 high-resolution mature mitoribosome analysis (nguyen2023structuralinsightsinto pages 3-4, singh2024mitoribosomestructurewith pages 5-6) | Major gaps are direct fly nucleotide mapping, endogenous protein localization, purified-enzyme kinetics, catalytic-dead fly rescue, and fly mtLSU structural analysis. |
Table: Evidence hierarchy for functional annotation of Drosophila melanogaster Mrm2/Q9VDT6, separating direct fly findings from orthologue-based mechanistic inference. It also highlights quantitative phenotypes and the principal unresolved experimental gaps.
The direct experimental paper identifies CG11447 as the D. melanogaster orthologue of MRM2 and calls it DmMRM2. This matches the supplied UniProt accession Q9VDT6, gene Mrm2, organism D. melanogaster, and mitochondrial-rRNA-methyltransferase description (rebeloguiomar2022alatestageassembly pages 7-8).
The protein-family assignment is coherent rather than merely name-based. MRM2 proteins belong to the FtsJ/RrmJ family of class-I-like SAM-dependent RNA methyltransferases. Human MRM2 contains the characteristic seven-β-strand methyltransferase fold and conserved residues surrounding the RNA- and SAM-binding sites; this is consistent with the supplied Q9VDT6 InterPro/Pfam annotations (rebeloguiomar2022alatestageassembly pages 5-7).
The gene symbol is potentially confusing across species. Human MRM2, also known as FTSJ2/RRMJ2, and bacterial RlmE/RrmJ/FtsJ are orthologues, not the target protein. Their results are used below only where explicitly labeled as orthologue-based inference. No evidence retrieved suggested that Q9VDT6 represents a different fly protein.
The enzymatic annotation supported by family conservation is:
S-adenosyl-L-methionine + uridine in mitochondrial large-subunit rRNA → S-adenosyl-L-homocysteine + 2′-O-methyluridine in mitochondrial rRNA.
Thus, dmMRM2 is predicted to transfer a methyl group from SAM to the 2′ hydroxyl of the ribose, not to the uracil base. The broad UniProt EC assignment 2.1.1.- is appropriate because Q9VDT6 itself has not been subjected to a published purified-enzyme kinetic or substrate-specificity assay. Human MRM2 is directly established as a SAM-dependent 2′-O-ribose methyltransferase (rebeloguiomar2022alatestageassembly pages 5-7).
In humans, MRM2 installs Um3039 in helix H92/the A-loop of mitochondrial 16S rRNA. Older literature numbers the same human rRNA residue as U1369, reflecting different coordinate conventions; these should not be interpreted as two substrates. The neighboring MRM3-dependent nucleotide is correspondingly reported as G3040 or G1370 (sanchez2020methylationofribosomal pages 7-8, rorbach2014mrm2andmrm3 pages 9-10, rebeloguiomar2022alatestageassembly pages 8-9).
The corresponding site lies in the mitochondrial large-subunit peptidyl-transferase center and is homologous to bacterial 23S-rRNA U2552. It participates in the A-loop environment that positions aminoacyl-tRNA during peptide-bond synthesis. Therefore, the likely dmMRM2 substrate is the homologous uridine in Drosophila mitochondrial large-subunit rRNA—not cytosolic rRNA, mRNA, or tRNA (sanchez2020methylationofribosomal pages 7-8, rebeloguiomar2022alatestageassembly pages 8-9).
Evidence qualification: the retrieved fly study did not directly map this modification in Drosophila mt-rRNA. Human U3039 is consequently a homologous reference position, not a literal fly coordinate. Direct fly RiboMeth-seq or RNA mass spectrometry remains necessary to establish the exact Q9VDT6 substrate nucleotide.
Current evidence indicates that MRM2 is more than a conventional “writer” enzyme. In human knockout cells, MRM2 absence traps mitochondrial large ribosomal subunits in late, non-translation-competent assembly states. A 2.6-Å cryo-EM analysis resolved five intermediates with disordered domains IV and V of 16S mt-rRNA, incomplete bL36m incorporation, and persistent binding of the MALSU1:L0R8F8:mtACP anti-association module (rebeloguiomar2022alatestageassembly pages 1-2, rebeloguiomar2022alatestageassembly pages 5-7).
Mechanistically, MRM2 binding promotes stabilization of H92 and repositioning/folding of H91 and H89. These changes form the mature intersubunit interface and bL36m-binding pocket. Retention of the anti-association module prevents immature mtLSU particles from joining the small subunit and entering translation, making this a quality-control checkpoint rather than merely a chemical-modification step (rebeloguiomar2022alatestageassembly pages 8-9, rebeloguiomar2022alatestageassembly pages 5-7).
The strongest evidence separating catalysis from assembly comes from human complementation. K59A and D154A substitutions abolished U3039 methylation, yet both catalytically inactive proteins restored mitochondrial translation. In control human mtLSU, approximately 70% of 16S rRNA carried Um3039/Gm3040 and approximately 30% carried unmethylated U3039 with Gm3040; nevertheless, the protein's physical assembly-factor role—not Um3039 formation alone—was essential for translation (rebeloguiomar2022alatestageassembly pages 5-7, rebeloguiomar2022alatestageassembly pages 7-8).
This makes the most useful primary annotation for dmMRM2: a late mtLSU biogenesis factor with predicted rRNA 2′-O-methyltransferase activity. The same bifunctional arrangement is strongly conserved, but catalytic-dead rescue has not yet been performed in flies.
A 2023 human structural study further placed the U3039/G3040 A-loop region in a coordinated maturation network involving GTPBP7 and GTPBP10. H89 accommodation is coupled to late incorporation of uL16m and bL36m, reinforcing the checkpoint model developed from MRM2-deficient particles (published 1 December 2023; https://doi.org/10.1038/s41467-023-43599-z) (nguyen2023structuralinsightsinto pages 3-4).
Q9VDT6 is annotated as a precursor, consistent with synthesis in the cytosol followed by mitochondrial import through an N-terminal targeting sequence. Its mature functional compartment is expected to be the mitochondrial matrix, because mitochondrial rRNA, RNA maturation, and mitoribosome assembly are matrix processes. Mitoribosome biogenesis begins near mitochondrial nucleoids and occurs substantially in neighboring mitochondrial RNA granules (MRGs) (rebeloguiomar2022alatestageassembly pages 1-2).
Human MRM2 localizes to mitochondria, associates with mitochondrial ribosomal material, and sediments particularly with the 39S large subunit (rorbach2014mrm2andmrm3 pages 9-10). For dmMRM2, the mitochondrial assignment is strongly supported by orthology, precursor annotation, and the mitochondrial respiratory phenotype. However, endogenous Q9VDT6 has not, in the retrieved literature, been localized by fly immunofluorescence, protease protection, or biochemical fractionation. “Mitochondrial matrix/assembling mtLSU, probably in or near MRGs” is therefore the appropriate evidence-weighted description.
The functional pathway is:
nuclear expression of Mrm2 → cytosolic synthesis and mitochondrial import → 16S mt-rRNA A-loop modification and late mtLSU folding → mature mitoribosome formation → translation of mtDNA-encoded respiratory-chain subunits → OXPHOS-complex assembly and mitochondrial respiration → developmental and tissue energy homeostasis.
MRM2 is not a conventional signaling molecule, and no specific receptor or second-messenger pathway is indicated. Its effects are transmitted biochemically through mitochondrial gene expression and bioenergetics. Mammalian mitochondria encode 13 core OXPHOS polypeptides, so broad inhibition of mitochondrial translation destabilizes complexes containing those products (rebeloguiomar2022alatestageassembly pages 1-2).
In human MRM2-knockout cells, average mitoribosome occupancy on mitochondrial mRNAs fell to 13.9% ± 7.6%. Respiratory-chain complexes I and III retained less than 30% of control activity, while complex IV activity was almost absent. These are human orthologue data, not fly measurements, but quantitatively demonstrate the expected consequence of blocking this assembly checkpoint (rebeloguiomar2022alatestageassembly pages 2-3).
The central fly evidence comes from Rebelo-Guiomar and colleagues, “A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit,” Nature Communications 13, 929, published 15 February 2022, DOI/URL: https://doi.org/10.1038/s41467-022-28503-5; PubMed 35177605 (rebeloguiomar2022alatestageassembly pages 1-2).
Ubiquitous RNAi against CG11447/dmMRM2 significantly reduced transcript abundance (n=3 control and n=4 knockdown biological data points; P=0.0019). Knockdown delayed development: few larvae reached pupation, most of those died during late pupation, and rare escapers were weak, malformed, or unable to complete eclosion. A second ubiquitous driver also produced lethality (rebeloguiomar2022alatestageassembly pages 7-8).
The timing is mechanistically informative. During pupation, flies transition from a relatively glycolytic larval state toward stronger reliance on mitochondrial respiration. Respiratory-chain subunits normally rose during the second half of pupation, whereas this increase was substantially blunted in dmMRM2-knockdown animals and coincided with developmental arrest. This supports failure of mitochondrial translation/OXPHOS capacity rather than an unrelated morphogenetic role (rebeloguiomar2022alatestageassembly pages 7-8, rebeloguiomar2022alatestageassembly pages 8-9).
Pan-neuronal dmMRM2 knockdown was lethal. Pan-muscular knockdown permitted adult emergence but caused a severe defect in startle-induced negative geotaxis, with 70 controls versus 56 knockdown flies and P<0.00001. These results demonstrate particular dependence of neuronal and muscular homeostasis on dmMRM2, consistent with the high energetic requirements of those tissues (rebeloguiomar2022alatestageassembly pages 7-8).
The study did not directly measure fly mitochondrial ribosome assembly, the fly rRNA methylation site, or fly mitochondrial translation rates. Accordingly, the causal sequence from dmMRM2 loss to mtLSU assembly failure is compelling but still partly orthology-based.
No direct 2023–2024 experimental publication specific to Q9VDT6/CG11447 was identified in the searches. The 2022 Nature Communications study remains the definitive direct functional study.
Recent work nevertheless strengthens the mechanistic context. The 2023 GTPBP10 cryo-EM study showed how H89 is held and subsequently accommodated during human mtLSU maturation, and linked this process to the U3039/G3040 A-loop region and sequential incorporation of late ribosomal proteins (published December 2023; https://doi.org/10.1038/s41467-023-43599-z) (nguyen2023structuralinsightsinto pages 3-4). A 2024 2.2-Å human mitoribosome structure provided an improved framework for interpreting rRNA modifications, cofactors, mRNA/tRNA positioning, and mature translation architecture (published May 2024; https://doi.org/10.1038/s41467-024-48163-x) (singh2024mitoribosomestructurewith pages 5-6).
A 2024 review of mitochondrial disorders emphasizes that defective mt-rRNA maturation and mitoribosome assembly commonly cause multisystem, especially neurodegenerative, disease and discusses dmMRM2 knockdown among relevant animal models (published May 2024; https://doi.org/10.3389/fcell.2024.1410245). These sources support the biological importance of the pathway but do not add direct biochemical evidence for Q9VDT6.
The immediate application of dmMRM2 is as a genetically tractable model of mitochondrial translation failure that secondarily impairs multiple OXPHOS complexes, rather than directly mutating an individual respiratory-chain component. Tissue-specific GAL4/RNAi manipulation permits comparison of neuronal, muscular, and whole-organism susceptibility. The late-pupal arrest also provides a model for studying how developmental metabolic transitions expose latent mitochondrial defects (rebeloguiomar2022alatestageassembly pages 8-9, rebeloguiomar2022alatestageassembly pages 9-10).
The model has translational relevance because pathogenic human MRM2 variants have been associated with MELAS-like mitochondrial disease, and the fly neuromuscular phenotypes reproduce the broad tissue classes commonly affected by mitochondrial cytopathies. It should not yet be treated as a validated drug-screening platform, however: no therapeutic rescue or compound-screening implementation was identified (rebeloguiomar2022alatestageassembly pages 7-8).
At a basic-research level, dmMRM2 offers a way to test whether the conserved methyltransferase protein functions chiefly as an RNA-modifying enzyme, an assembly scaffold, or both. A fly transgene carrying catalytic-site substitutions homologous to human K59A/D154A would be particularly decisive.
Mrm2/CG11447 encodes a nuclear-encoded mitochondrial FtsJ-family SAM-dependent rRNA uridine 2′-O-methyltransferase and probable late 39S mitoribosomal-subunit assembly factor. It is predicted to methylate the conserved H92/A-loop uridine of mitochondrial large-subunit rRNA and facilitates maturation of the peptidyl-transferase-center/inter-subunit interface. dmMRM2 is required for mitochondrial respiratory-chain homeostasis, development, and neuronal and muscular function.
The highest-priority experiments are: (1) map the exact Drosophila mt-rRNA modification by RiboMeth-seq and RNA LC–MS/MS; (2) assay recombinant Q9VDT6 against defined fly mt-rRNA substrates; (3) localize endogenous tagged dmMRM2 within mitochondria and MRGs; (4) rescue a fly null or RNAi phenotype with wild-type versus catalytic-dead dmMRM2; (5) quantify fly mitochondrial translation and respiratory-complex activity directly; and (6) structurally characterize dmMRM2-bound or dmMRM2-deficient fly mtLSU intermediates.
Overall, literature for this specific fly protein remains limited. The evidence is sufficient to assign dmMRM2 confidently to mitochondrial large-subunit rRNA maturation and mitochondrial translation, but claims about its exact catalytic site and structural action in Drosophila should remain explicitly marked as conserved-function inference rather than direct Q9VDT6 biochemistry.
References
(rebeloguiomar2022alatestageassembly pages 5-7): Pedro Rebelo-Guiomar, Simone Pellegrino, Kyle C Dent, Aldema Sas-Chen, Leonor Miller-Fleming, Caterina Garone, Lindsey Van Haute, Jack F Rogan, Adam Dinan, Andrew Firth, Byron Andrews, Alex Whitworth, Schraga Schwartz, Alan Warren, and Michal Minczuk. A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit. Text, Feb 2022. URL: https://doi.org/10.17863/cam.81567, doi:10.17863/cam.81567. This article has 54 citations and is from a peer-reviewed journal.
(rebeloguiomar2022alatestageassembly pages 7-8): Pedro Rebelo-Guiomar, Simone Pellegrino, Kyle C Dent, Aldema Sas-Chen, Leonor Miller-Fleming, Caterina Garone, Lindsey Van Haute, Jack F Rogan, Adam Dinan, Andrew Firth, Byron Andrews, Alex Whitworth, Schraga Schwartz, Alan Warren, and Michal Minczuk. A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit. Text, Feb 2022. URL: https://doi.org/10.17863/cam.81567, doi:10.17863/cam.81567. This article has 54 citations and is from a peer-reviewed journal.
(rebeloguiomar2022alatestageassembly pages 1-2): Pedro Rebelo-Guiomar, Simone Pellegrino, Kyle C Dent, Aldema Sas-Chen, Leonor Miller-Fleming, Caterina Garone, Lindsey Van Haute, Jack F Rogan, Adam Dinan, Andrew Firth, Byron Andrews, Alex Whitworth, Schraga Schwartz, Alan Warren, and Michal Minczuk. A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit. Text, Feb 2022. URL: https://doi.org/10.17863/cam.81567, doi:10.17863/cam.81567. This article has 54 citations and is from a peer-reviewed journal.
(rorbach2014mrm2andmrm3 pages 1-2): Joanna Rorbach, Pierre Boesch, Payam A. Gammage, Thomas J. J. Nicholls, Sarah F. Pearce, Dipali Patel, Andreas Hauser, Fabiana Perocchi, and Michal Minczuk. Mrm2 and mrm3 are involved in biogenesis of the large subunit of the mitochondrial ribosome. Molecular Biology of the Cell, 25:2542-2555, Sep 2014. URL: https://doi.org/10.1091/mbc.e14-01-0014, doi:10.1091/mbc.e14-01-0014. This article has 159 citations and is from a domain leading peer-reviewed journal.
(rebeloguiomar2022alatestageassembly pages 8-9): Pedro Rebelo-Guiomar, Simone Pellegrino, Kyle C Dent, Aldema Sas-Chen, Leonor Miller-Fleming, Caterina Garone, Lindsey Van Haute, Jack F Rogan, Adam Dinan, Andrew Firth, Byron Andrews, Alex Whitworth, Schraga Schwartz, Alan Warren, and Michal Minczuk. A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit. Text, Feb 2022. URL: https://doi.org/10.17863/cam.81567, doi:10.17863/cam.81567. This article has 54 citations and is from a peer-reviewed journal.
(rebeloguiomar2022alatestageassembly pages 2-3): Pedro Rebelo-Guiomar, Simone Pellegrino, Kyle C Dent, Aldema Sas-Chen, Leonor Miller-Fleming, Caterina Garone, Lindsey Van Haute, Jack F Rogan, Adam Dinan, Andrew Firth, Byron Andrews, Alex Whitworth, Schraga Schwartz, Alan Warren, and Michal Minczuk. A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit. Text, Feb 2022. URL: https://doi.org/10.17863/cam.81567, doi:10.17863/cam.81567. This article has 54 citations and is from a peer-reviewed journal.
(nguyen2023structuralinsightsinto pages 3-4): Thu Giang Nguyen, Christina Ritter, and Eva Kummer. Structural insights into the role of gtpbp10 in the rna maturation of the mitoribosome. Nature Communications, Dec 2023. URL: https://doi.org/10.1038/s41467-023-43599-z, doi:10.1038/s41467-023-43599-z. This article has 17 citations and is from a highest quality peer-reviewed journal.
(singh2024mitoribosomestructurewith pages 5-6): Vivek Singh, Yuzuru Itoh, Samuel Del’Olio, Asem Hassan, Andreas Naschberger, Rasmus Kock Flygaard, Yuko Nobe, Keiichi Izumikawa, Shintaro Aibara, Juni Andréll, Paul C. Whitford, Antoni Barrientos, Masato Taoka, and Alexey Amunts. Mitoribosome structure with cofactors and modifications reveals mechanism of ligand binding and interactions with l1 stalk. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48163-x, doi:10.1038/s41467-024-48163-x. This article has 39 citations and is from a highest quality peer-reviewed journal.
(sanchez2020methylationofribosomal pages 7-8): M. L. Sanchez, Miriam Cipullo, Miriam Cipullo, Shreekara Gopalakrishna, Shreekara Gopalakrishna, A. Khawaja, A. Khawaja, J. Rorbach, and J. Rorbach. Methylation of ribosomal rna: a mitochondrial perspective. Frontiers in Genetics, Jul 2020. URL: https://doi.org/10.3389/fgene.2020.00761, doi:10.3389/fgene.2020.00761. This article has 42 citations and is from a peer-reviewed journal.
(rorbach2014mrm2andmrm3 pages 9-10): Joanna Rorbach, Pierre Boesch, Payam A. Gammage, Thomas J. J. Nicholls, Sarah F. Pearce, Dipali Patel, Andreas Hauser, Fabiana Perocchi, and Michal Minczuk. Mrm2 and mrm3 are involved in biogenesis of the large subunit of the mitochondrial ribosome. Molecular Biology of the Cell, 25:2542-2555, Sep 2014. URL: https://doi.org/10.1091/mbc.e14-01-0014, doi:10.1091/mbc.e14-01-0014. This article has 159 citations and is from a domain leading peer-reviewed journal.
(rebeloguiomar2022alatestageassembly pages 9-10): Pedro Rebelo-Guiomar, Simone Pellegrino, Kyle C Dent, Aldema Sas-Chen, Leonor Miller-Fleming, Caterina Garone, Lindsey Van Haute, Jack F Rogan, Adam Dinan, Andrew Firth, Byron Andrews, Alex Whitworth, Schraga Schwartz, Alan Warren, and Michal Minczuk. A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit. Text, Feb 2022. URL: https://doi.org/10.17863/cam.81567, doi:10.17863/cam.81567. This article has 54 citations and is from a peer-reviewed journal.