Evidence map›Paper›PMID 17901157›Full record

ArticleRNA (New York, N.Y.)2007

Roles of the negatively charged N-terminal extension of Saccharomyces cerevisiae ribosomal protein S5 revealed by characterization of a yeast strain containing human ribosomal protein S5.

Oleksandr Galkin, Amber A Bentley, Sujatha Gupta, Beth-Ann Compton, Barsanjit Mazumder, Terri Goss Kinzy, William C Merrick, Maria Hatzoglou, Tatyana V Pestova, Christopher U T Hellen and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

23 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function.International journal of molecular sciences · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Tricks an IRES uses to enslave ribosomes.Trends in microbiology · 2012
    Review
  16. Ribosome recycling step in yeast cytoplasmic protein synthesis is catalyzed by eEF3 and ATP.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  17. Article
  18. Article
  19. Article
  20. 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

11 authors at 3 institutions in 1 country.

Oleksandr GalkinDepartment of Biological, Geological and Environmental Sciences, Cleveland State University, Cleveland, Ohio 44115, USA.
Amber A Bentley
Sujatha Gupta
Beth-Ann Compton
Barsanjit Mazumder
Terri Goss Kinzy
William C Merrick
Maria Hatzoglou
Tatyana V Pestova
Christopher U T Hellen
Anton A Komar
Cleveland State University · USCase Western Reserve University · USState University of New York · US

Funding

Translational Control by NutrientsR01DK060596 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI MARIA HATZOGLOU · 2002 to 2026
$6.3M
Regulators of Translation Elongation Factor eEF1AR01GM057483 · NIGMS · WESTERN MICHIGAN UNIVERSITY · PI KINZY, TERRI GOSS · 1998 to 2017
$5.4M
Translational Control by Osmotically Active SolutesR37DK060596 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI HATZOGLOU, MARIA · 2011 to 2020
$5.3M
Translational Silencing in Monocytes: Role of L13aR01HL079164 · NHLBI · CLEVELAND STATE UNIVERSITY · PI MAZUMDER, BARSANJIT · 2005 to 2019
$4.5M
IRES-mediated translation initiation on viral mRNAsR01AI051340 · NIAID · SUNY DOWNSTATE MEDICAL CENTER · PI HELLEN, CHRISTOPHER ULRICH TRISTRAM · 2002 to 2013
$3.6M
Yeast eLF2A: A Suppressor of Internal InitiationR01GM068079 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI MERRICK, WILLIAM C. · 2004 to 2007
$1.1M
IRES-mediated translation initiation on viral mRNAsR56AI051340 · NIAID · SUNY DOWNSTATE MEDICAL CENTER · PI HELLEN, CHRISTOPHER ULRICH TRISTRAM · 2008 to 2015
$856k
NHLBI NIH HHS HL79164NHLBI NIH HHS R01 HL079164NIAID NIH HHS AI-51340NIAID NIH HHS R01 AI051340NIAID NIH HHS R56 AI051340NIDDK NIH HHS DK60596NIDDK NIH HHS R01 DK060596NIDDK NIH HHS R37 DK060596NIGMS NIH HHS GM57483NIGMS NIH HHS GM68079NIGMS NIH HHS R01 GM057483NIGMS NIH HHS R01 GM068079
6 · The paper itself

Abstract

Ribosomal protein (rp) S5 belongs to a family of ribosomal proteins that includes bacterial rpS7. rpS5 forms part of the exit (E) site on the 40S ribosomal subunit and is essential for yeast viability. Human rpS5 is 67% identical and 79% similar to Saccharomyces cerevisiae rpS5 but lacks a negatively charged (pI approximately 3.27) 21 amino acid long N-terminal extension that is present in fungi. Here we report that replacement of yeast rpS5 with its human homolog yielded a viable yeast strain with a 20%-25% decrease in growth rate. This replacement also resulted in a moderate increase in the heavy polyribosomal components in the mutant strain, suggesting either translation elongation or termination defects, and in a reduction in the polyribosomal association of the elongation factors eEF3 and eEF1A. In addition, the mutant strain was characterized by moderate increases in +1 and -1 programmed frameshifting and hyperaccurate recognition of the UAA stop codon. The activities of the cricket paralysis virus (CrPV) IRES and two mammalian cellular IRESs (CAT-1 and SNAT-2) were also increased in the mutant strain. Consistently, the rpS5 replacement led to enhanced direct interaction between the CrPV IRES and the mutant yeast ribosomes. Taken together, these data indicate that rpS5 plays an important role in maintaining the accuracy of translation in eukaryotes and suggest that the negatively charged N-terminal extension of yeast rpS5 might affect the ribosomal recruitment of specific mRNAs.

Indexed as

Base SequenceHumansModels, MolecularMolecular Sequence DataMutagenesisNucleic Acid ConformationRibosomal ProteinsRibosomesRNA, FungalRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTransfectionRibosomal Proteinsribosomal protein S5RNA, FungalRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID17901157
PMCPMC2080588
OpenAlexW2107031430

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.