Evidence map›Paper›PMID 37186227›Full record

ArticleMicrobiologyOpen2023

Highly efficient export of a disulfide-bonded protein to the periplasm and medium by the Tat pathway using CyDisCo in Escherichia coli.

Klaudia Arauzo-Aguilera, Mirva J Saaranen, Colin Robinson, Lloyd W Ruddock

Open access · goldAbstract read
In one paragraph

Article in MicrobiologyOpen, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed, 1 pooled it
2.5field-weighted citation impact, top 12% 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

10 citing papers in PubMed, 1 synthesis or guideline pooled it, 10 citations in OpenAlex.

  1. Pooled it
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  5. Article
  6. Review
  7. Review
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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 2 institutions in 2 countries.

Klaudia Arauzo-AguileraSchool of Biosciences, University of Kent, Canterbury, UK.
Mirva J SaaranenFaculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.
Colin RobinsonSchool of Biosciences, University of Kent, Canterbury, UK.ORCID 0000-0002-1739-032X
Lloyd W RuddockFaculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.ORCID 0000-0002-6247-686X
University of Kent · GBUniversity of Oulu · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High-value heterologous proteins produced in Escherichia coli that contain disulfide bonds are almost invariably targeted to the periplasm via the Sec pathway as it, among other advantages, enables disulfide bond formation and simplifies downstream processing. However, the Sec system cannot transport complex or rapidly folding proteins, as it only transports proteins in an unfolded state. The Tat system also transports proteins to the periplasm, and it has significant potential as an alternative means of recombinant protein production because it transports fully folded proteins. Most of the studies related to Tat secretion have used the well-studied TorA signal peptide that is Tat-specific, but this signal peptide also tends to induce degradation of the protein of interest, resulting in lower yields. This makes it difficult to use Tat in the industry. In this study, we show that a model disulfide bond-containing protein, YebF, can be exported to the periplasm and media at a very high level by the Tat pathway in a manner almost completely dependent on cytoplasmic disulfide formation, by other two putative Tat SPs: those of MdoD and AmiC. In contrast, the TorA SP exports YebF at a low level.

Indexed as

Escherichia coliEscherichia coli ProteinsPeriplasmRecombinant ProteinsTwin-Arginine-Translocation SystemCulture MediaDisulfidesOxidoreductases, N-DemethylatingProtein FoldingProtein Sorting SignalsProtein TransportCulture MediaDisulfidesEscherichia coli ProteinsOxidoreductases, N-DemethylatingProtein Sorting SignalsRecombinant Proteinstrimethylamine dehydrogenaseTwin-Arginine-Translocation SystemYebF protein, E coliCyDisCodisulfide bondEscherichia coliperiplasmsignal peptideTat pathway

Identifiers

PMID37186227
PMCPMC9995818
OpenAlexW4323668293

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.