Evidence map›Paper›PMID 27390266›Full record

ArticleRNA (New York, N.Y.)2016

The N-terminal extension of yeast ribosomal protein L8 is involved in two major remodeling events during late nuclear stages of 60S ribosomal subunit assembly.

Beril Tutuncuoglu, Jelena Jakovljevic, Shan Wu, Ning Gao, John L Woolford

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024
    Article
  3. Review
  4. Archaea/eukaryote-specific ribosomal proteins - guardians of a complex structure.Computational and structural biotechnology journal · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. 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

5 authors at 2 institutions in 2 countries.

Beril TutuncuogluDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
Jelena JakovljevicDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
Shan WuSchool of Life Sciences, Tsinghua University, Beijing, 100084, China.
Ning GaoSchool of Life Sciences, Tsinghua University, Beijing, 100084, China.
John L WoolfordDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA jw17@andrew.cmu.edu.
Carnegie Mellon University · USTsinghua University · CN

Funding

YEAST RIBOSOME BIOGENESISR01GM028301 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI WOOLFORD, JOHN L. · 1985 to 2025
$8.4M
NIGMS NIH HHS R01 GM028301
6 · The paper itself

Abstract

Assaying effects on pre-rRNA processing and ribosome assembly upon depleting individual ribosomal proteins (r-proteins) provided an initial paradigm for assembly of eukaryotic ribosomes in vivo-that each structural domain of ribosomal subunits assembles in a hierarchical fashion. However, two features suggest that a more complex pathway may exist: (i) Some r-proteins contain extensions that reach long distances across ribosomes to interact with multiple rRNA domains as well as with other r-proteins. (ii) Individual r-proteins may assemble in a stepwise fashion. For example, the globular domain of an r-protein might assemble separately from its extensions. Thus, these extensions might play roles in assembly that could not be revealed by depleting the entire protein. Here, we show that deleting or mutating extensions of r-proteins L7 (uL30) and L35 (uL29) from yeast reveal important roles in early and middle steps during 60S ribosomal subunit biogenesis. Detailed analysis of the N-terminal terminal extension of L8 (eL8) showed that it is necessary for late nuclear stages of 60S subunit assembly involving two major remodeling events: removal of the ITS2 spacer; and reorganization of the central protuberance (CP) containing 5S rRNA and r-proteins L5 (uL18) and L11 (uL5). Mutations in the L8 extension block processing of 7S pre-rRNA, prevent release of assembly factors Rpf2 and Rrs1 from pre-ribosomes, which is required for rotation of the CP, and block association of Sda1, the Rix1 complex, and the Rea1 ATPase involved in late steps of remodeling.

Indexed as

Amino Acid MotifsCell Cycle ProteinsNuclear ProteinsProtein BindingRibosomal ProteinsRibosome Subunits, Large, EukaryoticRNA-Binding ProteinsRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsNuclear ProteinsRibosomal ProteinsRix1 protein, S cerevisiaeRNA-Binding ProteinsRNA, RibosomalRPF2 protein, S cerevisiaeRRS1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSDA1 protein, S cerevisiaepre-ribosome remodelingribosomal protein extensionsribosome assemblyrRNA

Identifiers

PMID27390266
PMCPMC4986894
OpenAlexW2465128212

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.