Evidence map›Paper›PMID 34713496›Full record

ArticleYeast (Chichester, England)2022

Functional analyses of mitoribosome 54S subunit devoid of mitochondria-specific protein sequences.

Barbara Santos, Rui Zeng, Sasa F Jorge, Jose Ribamar Ferreira-Junior, Antoni Barrientos, Mario H Barros

Open access · greenAbstract read
In one paragraph

Article in Yeast (Chichester, England), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Barbara SantosDepartamento de Microbiologia, Universidade de São Paulo, São Paulo, Brazil.ORCID 0000-0001-6620-3618
Rui ZengDepartment of Neurology, University of Miami Miller School of Medicine, Miami, Florida, USA.
Sasa F JorgeDepartamento de Microbiologia, Universidade de São Paulo, São Paulo, Brazil.
Jose Ribamar Ferreira-JuniorEscola de Artes, Ciências e Humanidades, Universidade de São Paulo, São Paulo, Brazil.ORCID 0000-0001-5539-5298
Antoni BarrientosDepartment of Neurology, University of Miami Miller School of Medicine, Miami, Florida, USA.ORCID 0000-0001-9018-3231
Mario H BarrosDepartamento de Microbiologia, Universidade de São Paulo, São Paulo, Brazil.ORCID 0000-0003-2977-9815
Universidade de São Paulo · BRUniversity of Miami · US

Funding

Mitochondrial Biogenesis in Health and DiseaseR35GM118141 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BARRIENTOS, ANTONI · 2016 to 2025
$8.9M
NIGMS NIH HHS R35 GM118141NIH HHS R35-GM118141
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, mitoribosomes are composed of a 54S large subunit (mtLSU) and a 37S small subunit (mtSSU). The two subunits altogether contain 73 mitoribosome proteins (MRPs) and two ribosomal RNAs (rRNAs). Although mitoribosomes preserve some similarities with their bacterial counterparts, they have significantly diverged by acquiring new proteins, protein extensions, and new RNA segments, adapting the mitoribosome to the synthesis of highly hydrophobic membrane proteins. In this study, we investigated the functional relevance of mitochondria-specific protein extensions at the C-terminus (C) or N-terminus (N) present in 19 proteins of the mtLSU. The studied mitochondria-specific extensions consist of long tails and loops extending from globular domains that mainly interact with mitochondria-specific proteins and 21S rRNA moieties extensions. The expression of variants devoid of extensions in uL4 (C), uL5 (N), uL13 (N), uL13 (C), uL16 (C), bL17 (N), bL17 (C), bL21 (24), uL22 (N), uL23 (N), uL23 (C), uL24 (C), bL27 (C), bL28 (N), bL28 (C), uL29 (N), uL29 (C), uL30 (C), bL31 (C), and bL32 (C) did not rescue the mitochondrial protein synthesis capacities and respiratory growth of the respective null mutants. On the contrary, the truncated form of the mitoribosome exit tunnel protein uL24 (N) yields a partially functional mitoribosome. Also, the removal of mitochondria-specific sequences from uL1 (N), uL3 (N), uL16 (N), bL9 (N), bL19 (C), uL29 (C), and bL31 (N) did not affect the mitoribosome function and respiratory growth. The collection of mutants described here provides new means to study and evaluate defective assembly modules in the mitoribosome biogenesis process.

Indexed as

MitochondriaMitochondrial RibosomesMitochondrial ProteinsProtein BiosynthesisRibosomal ProteinsSaccharomyces cerevisiaeMitochondrial ProteinsRibosomal Proteinsmitochondria-specific extensionsmitoribosome 54S subunitSaccharomyces cerevisiae

Identifiers

PMID34713496
PMCPMC8969203
OpenAlexW3208378036

What OpenQuestion holds

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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.