Evidence map›Paper›PMID 9371808›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

TnTIN and TnTAP: mini-transposons for site-specific proteolysis in vivo.

M Ehrmann, P Bolek, M Mondigler, D Boyd, R Lange

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

17 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Outer membrane lipoprotein biogenesis: Lol is not the end.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Target-directed proteolysis at the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Prediction by a neural network of outer membrane beta-strand protein topology.Protein science : a publication of the Protein Society · 1998
    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

5 authors at 1 institution in 2 countries.

M EhrmannFakultät für Biologie, Universität Konstanz, Germany. mechael.ehrmann@uni-konstanz.de
P Bolek
M Mondigler
D Boyd
R Lange
Harvard University · US

Funding

Microbial Diversity in Mechanisms of Disulfide Bond Formation and ReductionR01GM041883 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BOYD, DANA · 1989 to 2014
$7.8M
STUDIES OF TRANSMEMBRANE HELIX-HELIX ASSOCIATIONP01GM054160 · NIGMS · YALE UNIVERSITY · PI ENGELMAN, DONALD M · 1996 to 2003
$2.9M
NIGMS NIH HHS GM41883NIGMS NIH HHS GM54160NIGMS NIH HHS P01 GM054160NIGMS NIH HHS R01 GM041883
6 · The paper itself

Abstract

Tobacco etch virus (TEV) protease recognizes a 7-aa consensus sequence, Glu-Xaa-Xaa-Tyr-Xaa-Gln-Ser, where Xaa can be almost any amino acyl residue. Cleavage occurs between the conserved Gln and Ser residues. Because of its distinct specificity, TEV protease can be expressed in the cytoplasm without interfering with viability. Polypeptides that are not natural substrates of TEV protease are proteolyzed if they carry the appropriate cleavage site. Thus, this protease can be used to study target proteins in their natural environment in vivo, as well as in vitro. We describe two TnS-based mini-transposons that insert TEV protease cleavage sites at random into target proteins. TnTIN introduces TEV cleavage sites into cytoplasmic proteins. TnTAP facilitates the same operation for proteins localized to the bacterial cell envelope. By using two different target proteins, SecA and TolC, we show that such modified proteins can be cleaved in vivo and in vitro by TEV protease. Possible applications of the site-specific proteolysis approach are topological studies of soluble as well as of inner and outer membrane proteins, protein inactivation, insertion mutagenesis experiments, and protein tagging.

Indexed as

DNA Transposable ElementsEscherichia coli ProteinsMembrane Transport ProteinsAdenosine TriphosphatasesAmino Acid SequenceBacterial ProteinsEndopeptidasesHydrolysisMolecular Sequence DataSecA ProteinsSEC Translocation ChannelsAdenosine TriphosphatasesBacterial ProteinsDNA Transposable ElementsEndopeptidasesEscherichia coli ProteinsMembrane Transport ProteinsSecA ProteinsSEC Translocation ChannelsTEV protease

Identifiers

PMID9371808
PMCPMC24271
OpenAlexW2020063118

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.