Evidence map›Paper›PMID 15302932›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Translation arrest of SecM is essential for the basal and regulated expression of SecA.

Akiko Murakami, Hitoshi Nakatogawa, Koreaki Ito

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

33 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Ddi1 is a ubiquitin-dependent protease.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Frontiers in bioengineering and biotechnology · 2019
    Article
  15. Genome scale analysis of Escherichia coli with a comprehensive prokaryotic sequence-based biophysical model of translation initiation and elongation.DNA research : an international journal for rapid publication of reports on genes and genomes · 2018
    Article
  16. Article
  17. Article
  18. The ribosome and its role in protein folding: looking through a magnifying glass.Acta crystallographica. Section D, Structural biology · 2017
    Review
  19. Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. Mechanisms of ribosome rescue in bacteria.Nature reviews. Microbiology · 2015
    Review
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

3 authors at 2 institutions in 1 country.

Akiko MurakamiInstitute for Virus Research and Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Kyoto University, Kyoto 606-8507, Japan.
Hitoshi Nakatogawa
Koreaki Ito
Japan Science and Technology Agency · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SecM protein of Escherichia coli contains an arrest sequence (F(150)XXXXWIXXXXGIRAGP(166)), which interacts with the ribosomal exit tunnel to halt translation elongation beyond Pro-166. This inhibition is reversed by active export of the nascent SecM chain. Here, we studied the physiological roles of SecM. Arrest-alleviating mutations in the arrest sequence reduced the expression of secA, a downstream gene on the same mRNA. Among such mutations, the arrest-abolishing P166A substitution mutation on the chromosomal secM gene proved lethal unless the mutant cells are complemented with excess SecA. Whereas secretion defect due either to azide addition, a secY mutation, or low temperature leads to up-regulated SecA biosynthesis, this regulation was lost by a secM mutation, which synergistically retarded growth of cells with lowered secretion activity. Finally, an arrest-alleviating rRNA mutation affecting the constricted part of the exit tunnel lowered the basal level of SecA as well as its secretion defect-induced up-regulation. Thus, the arrest sequence of SecM has at least two roles in SecA translation. First, the transient elongation arrest in normal cells is required for the synthesis of SecA at levels sufficient to support cell growth. Second, the prolonged SecM elongation arrest under conditions of unfavorable protein secretion is required for the enhanced expression of SecA to cope with such conditions.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceBacterial ProteinsBase SequenceCold TemperatureDNA, BacterialEscherichia coliEscherichia coli ProteinsGene ExpressionGenes, BacterialMembrane Transport ProteinsMolecular Sequence DataMutationProtein BiosynthesisRibosomesSecA ProteinsAdenosine TriphosphatasesBacterial ProteinsDNA, BacterialEscherichia coli ProteinsMembrane Transport ProteinsSecA ProteinsSEC Translocation Channels

Identifiers

PMID15302932
PMCPMC514405
OpenAlexW2072172236

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.