Evidence map›Paper›PMID 12417577›Full record

ArticleThe Journal of cell biology2002

Accumulation of endoplasmic membranes and novel membrane-bound ribosome-signal recognition particle receptor complexes in Escherichia coli.

Anat A Herskovits, Eyal Shimoni, Abraham Minsky, Eitan Bibi

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

24 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
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  3. Little reason to call them small noncoding RNAs.Frontiers in microbiology · 2023
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  15. Evolution: like any other science it is predictable.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2010
    Article
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  17. Article
  18. Biogenesis of bacterial membrane vesicles.Molecular microbiology · 2009
    Article
  19. Studying membrane proteins through the eyes of the genetic code revealed a strong uracil bias in their coding mRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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

4 authors at 1 institution in 1 country.

Anat A HerskovitsDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Eyal Shimoni
Abraham Minsky
Eitan Bibi
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Escherichia coli, ribosomes must interact with translocons on the membrane for the proper integration of newly synthesized membrane proteins, cotranslationally. Previous in vivo studies indicated that unlike the E. coli signal recognition particle (SRP), the SRP receptor FtsY is required for membrane targeting of ribosomes. Accordingly, a putative SRP-independent, FtsY-mediated ribosomal targeting pathway has been suggested (Herskovits, A.A., E.S. Bochkareva, and E. Bibi. 2000. Mol. Microbiol. 38:927-939). However, the nature of the early contact of ribosomes with the membrane, and the involvement of FtsY in this interaction are unknown. Here we show that in cells depleted of the SRP protein, Ffh or the translocon component SecE, the ribosomal targeting pathway is blocked downstream and unprecedented, membrane-bound FtsY-ribosomal complexes are captured. Concurrently, under these conditions, novel, ribosome-loaded intracellular membrane structures are formed. We propose that in the absence of a functional SRP or translocon, ribosomes remain jammed at their primary membrane docking site, whereas FtsY-dependent ribosomal targeting to the membrane continues. The accumulation of FtsY-ribosome complexes induces the formation of intracellular membranes needed for their quantitative accommodation. Our results with E. coli, in conjunction with recent observations made with the yeast Saccharomyces cerevisiae, raise the possibility that the SRP receptor-mediated formation of intracellular membrane networks is governed by evolutionarily conserved principles.

Indexed as

Bacterial ProteinsCell FractionationEndoplasmic ReticulumEscherichia coliEscherichia coli ProteinsLuminescent ProteinsMacromolecular SubstancesMembrane LipidsMembrane ProteinsMicroscopy, ConfocalReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsRibosomal ProteinsRibosomesSEC Translocation ChannelsSignal Recognition ParticleBacterial ProteinsEscherichia coli ProteinsFtsY protein, BacteriaLuminescent ProteinsMacromolecular SubstancesMembrane LipidsMembrane ProteinsReceptors, Cytoplasmic and NuclearRecombinant Fusion Proteinsribosomal protein L1Ribosomal ProteinsSecE protein, E coliSEC Translocation ChannelsSignal Recognition Particleyellow fluorescent protein, Bacteria

Identifiers

PMID12417577
PMCPMC2173083
OpenAlexW2012474081

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.