Evidence map›Paper›PMID 24799711›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosome.

Prem S Kaushal, Manjuli R Sharma, Timothy M Booth, Emdadul M Haque, Chang-Shung Tung, Karissa Y Sanbonmatsu, Linda L Spremulli, Rajendra K Agrawal

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.4field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 79 citations in OpenAlex.

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  18. Structural insights into unique features of the human mitochondrial ribosome recycling.Proceedings of the National Academy of Sciences of the United States of America · 2019
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Prem S KaushalDivision of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY 12201;
Manjuli R SharmaDivision of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY 12201;
Timothy M BoothDivision of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY 12201;
Emdadul M HaqueDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599;
Chang-Shung TungTheoretical Biology and Biophysics, Theoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545; and.
Karissa Y SanbonmatsuTheoretical Biology and Biophysics, Theoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545; and.
Linda L SpremulliDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599;
Rajendra K AgrawalDivision of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY 12201;Department of Biomedical Sciences, School of Public Health, University at Albany, State University of New York, Albany, NY 12222 agrawal@wadsworth.org.
Wadsworth Center · USLos Alamos National Laboratory · USUniversity of North Carolina at Chapel Hill · US

Funding

Structural Aspects of Protein Synthesis in the Mammalian MitochondriaR01GM061576 · NIGMS · WADSWORTH CENTER · PI AGRAWAL, RAJENDRA K · 2001 to 2018
$6.4M
Large-Scale Simulations of Ribosomal DecodingR01GM072686 · NIGMS · UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB · PI SANBONMATSU, KARISSA Y · 2005 to 2024
$5.5M
NIGMS NIH HHS R01 GM061576NIGMS NIH HHS R01 GM072686
6 · The paper itself

Abstract

The mammalian mitochondrial ribosomes (mitoribosomes) are responsible for synthesizing 13 membrane proteins that form essential components of the complexes involved in oxidative phosphorylation or ATP generation for the eukaryotic cell. The mammalian 55S mitoribosome contains significantly smaller rRNAs and a large mass of mitochondrial ribosomal proteins (MRPs), including large mito-specific amino acid extensions and insertions in MRPs that are homologous to bacterial ribosomal proteins and an additional 35 mito-specific MRPs. Here we present the cryo-EM structure analysis of the small (28S) subunit (SSU) of the 55S mitoribosome. We find that the mito-specific extensions in homologous MRPs generally are involved in inter-MRP contacts and in contacts with mito-specific MRPs, suggesting a stepwise evolution of the current architecture of the mitoribosome. Although most of the mito-specific MRPs and extensions of homologous MRPs are situated on the peripheral regions, they also contribute significantly to the formation of linings of the mRNA and tRNA paths, suggesting a tailor-made structural organization of the mito-SSU for the recruitment of mito-specific mRNAs, most of which do not possess a 5' leader sequence. In addition, docking of previously published coordinates of the large (39S) subunit (LSU) into the cryo-EM map of the 55S mitoribosome reveals that mito-specific MRPs of both the SSU and LSU are involved directly in the formation of six of the 15 intersubunit bridges.

Indexed as

AnimalsBinding SitesCattleCryoelectron MicroscopyCytoplasmGTP-Binding ProteinsImage Processing, Computer-AssistedLiverMitochondriaProtein ConformationRibosomal ProteinsRibosomesRNA, MessengerRNA, Ribosomal, 16SRNA, TransferGTP-Binding ProteinsRibosomal ProteinsRNA, MessengerRNA, Ribosomal, 16SRNA, Transfercryo-electron microscopymammalian mitochondrial ribosomal SSUmammalian MRPsmito-12S rRNA

Identifiers

PMID24799711
PMCPMC4034187
OpenAlexW2022955673

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.