Evidence map›Paper›PMID 17911096›Full record

ArticleThe Journal of biological chemistry2007

Functional SmpB-ribosome interactions require tmRNA.

Thomas R Sundermeier, A Wali Karzai

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Ends of the line for tmRNA-SmpB.Frontiers in microbiology · 2014
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The tmRNA ribosome-rescue system.Advances in protein chemistry and structural biology · 2012
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Quality control of bacterial mRNA decoding and decay.Biochimica et biophysica acta · 2008
    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

2 authors at 2 institutions in 3 countries.

Thomas R SundermeierDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794, USA.
A Wali Karzai
Institute of Molecular and Cell Biology · RUStony Brook University · US

Funding

Virulence Mechanism of Y. pestis and tularensisP01AI055621 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI BENACH, JORGE L. · 2004 to 2010
$20.7M
Quality Control of Protein TranslationR01GM065319 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI KARZAI, A. WALI · 2002 to 2012
$2.5M
Quality Control of Protein TranslationR56GM065319 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI KARZAI, A. WALI · 2008 to 2008
$262k
NIAID NIH HHS AI055621NIAID NIH HHS P01 AI055621NIGMS NIH HHS GM65319NIGMS NIH HHS R01 GM065319NIGMS NIH HHS R56 GM065319
6 · The paper itself

Abstract

Small protein B (SmpB) is a requisite component of the transfer messenger RNA (tmRNA)-mediated bacterial translational quality control system known as trans-translation. The initial binding of tmRNA and its subsequent accommodation into the ribosomal A-site are activities intimately linked to SmpB protein function. From a mechanistic perspective, two key unanswered questions that require further investigation are: 1) what constitutes a stalled ribosome recognition complex and 2) does SmpB pre-bind ribosomes to recruit tmRNA. We have assessed, both in vivo and in vitro, the nature and stability of free SmpB interactions with stalled ribosomes and examined whether these interactions are functionally relevant. We present evidence to demonstrate that interaction of free SmpB with ribosomes is salt sensitive and significantly more labile than interaction of the SmpB.tmRNA complex with ribosomes. Upon dissociation of 70 S ribosomes SmpB partitions primarily with tmRNA rather than ribosomal subunits. This finding is consistent with biochemical and structural data demonstrating that tmRNA is the high-affinity binding partner of SmpB. Moreover, we show that under normal physiological conditions roughly similar numbers of SmpB and tmRNA molecules are present in cells. Our investigations also reveal that upon induction of a nonstop mRNA, SmpB is enriched in stalled ribosome fractions only in the presence of tmRNA. Based on these findings, we conclude that SmpB does not pre-bind stalled ribosome and that functional SmpB-stalled ribosome interactions require tmRNA. We propose that a 1:1:1 complex of SmpB.tmRNA.EF-Tu(GTP) recognizes and binds a stalled ribosome to initiate trans-translation.

Indexed as

BiochemistryCryoelectron MicroscopyDose-Response Relationship, DrugGuanosine TriphosphateProtein BiosynthesisRibosomal ProteinsRibosomesRibosome SubunitsRNARNA, BacterialRNA-Binding ProteinsSaltsThermusGuanosine TriphosphateRibosomal ProteinsRNARNA, BacterialRNA-Binding ProteinsSaltssmall protein BtmRNA

Identifiers

PMID17911096
PMCPMC2570653
OpenAlexW2080542254

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.