Evidence map›Paper›PMID 8190079›Full record

ArticleMolecular & general genetics : MGG1994

Genetic analysis of SecY: additional export-defective mutations and factors affecting their phenotypes.

T Taura, Y Akiyama, K Ito

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Article in Molecular & general genetics : MGG, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

  1. Article
  2. Article
  3. Lateral gate dynamics of the bacterial translocon during cotranslational membrane protein insertion.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
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  11. Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  12. Article
  13. Article
  14. Article
  15. Translation arrest of SecM is essential for the basal and regulated expression of SecA.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  16. Article
  17. Article
  18. Importance of transmembrane segments in Escherichia coli SecY.Molecular genetics and genomics : MGG · 2003
    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

3 authors.

T TauraDepartment of Cell Biology, Kyoto University, Japan.
Y Akiyama
K Ito

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A number of secY mutants of Escherichia coli showing protein export defects were isolated by a combination of localized mutagenesis and secA-lacZ screening. Most of them were cold sensitive and contained single base substitutions in secY leading to amino acid replacements in various parts of the SecY protein, mainly in the cytoplasmic and the transmembrane domains. A temperature-sensitive mutant with an export defect had the same base substitution as secY24, which was characterized previously. Many cold-sensitive secY mutants exhibited rapid responses to temperature lowering but their apparent defects varied at the permissive temperature. Others exhibited delayed responses to the temperature shift. Some secY mutations, including secY39, interfered with protein export when expressed from a multicopy plasmid, even in the presence of wild-type secY on the chromosome. Such "dominant negative" mutations, including secY-d1, which was studied previously, were all located in either cytoplasmic domain 5 or 6, which is consistent with our previous proposal that the C-terminal region of SecY is important for its function as a protein translocator. We also studied the phenotypes of strains in which one of the secY mutations was combined with the components of the secD operon. Overexpression of secD partially suppressed the secY39 mutation, while overexpression of secF exacerbated the export defects of secY122 and secY125 mutations. Overexpression of "yajC", located within the secD operon, suppressed secY-d1. Although yajC itself proved to be dispensable, its disruption impaired the growth of the secY39 mutant at 42 degrees C. These observations suggest that SecY interacts with SecD, SecF, and the product of yajC.

Indexed as

Escherichia coli ProteinsMutationAmino Acid SequenceBacterial ProteinsBase SequenceEscherichia coliMolecular Sequence DataSEC Translocation ChannelsTemperatureTranslocation, GeneticBacterial ProteinsEscherichia coli ProteinsSEC Translocation ChannelsSecY protein, E coli

Identifiers

PMID8190079

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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.