Evidence map›Paper›PMID 29103168›Full record

ArticleApplied microbiology and biotechnology2018

Fusion of DNA-binding domain of Pyrococcus furiosus ligase with TaqStoffel DNA polymerase as a useful tool in PCR with difficult targets.

Marta Śpibida, Beata Krawczyk, Beata Zalewska-Piątek, Rafał Piątek, Magdalena Wysocka, Marcin Olszewski

Open access · hybridAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.3field-weighted citation impact, top 39% 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, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. A Fusion of Taq DNA Polymerase with the CL7 Protein fromMolecules (Basel, Switzerland) · 2024
    Article
  6. Article
  7. Review
  8. Article
  9. PCR inhibition in qPCR, dPCR and MPS-mechanisms and solutions.Analytical and bioanalytical chemistry · 2020
    Review
  10. Engineering Polymerases for New Functions.Trends in biotechnology · 2019
    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

6 authors at 1 institution in 1 country.

Marta ŚpibidaDepartment of Molecular Biotechnology and Microbiology, Gdańsk University of Technology, ul. G. Narutowicza 11/12, 80-233, Gdańsk, Poland.
Beata KrawczykDepartment of Molecular Biotechnology and Microbiology, Gdańsk University of Technology, ul. G. Narutowicza 11/12, 80-233, Gdańsk, Poland.
Beata Zalewska-PiątekDepartment of Molecular Biotechnology and Microbiology, Gdańsk University of Technology, ul. G. Narutowicza 11/12, 80-233, Gdańsk, Poland.
Rafał PiątekDepartment of Molecular Biotechnology and Microbiology, Gdańsk University of Technology, ul. G. Narutowicza 11/12, 80-233, Gdańsk, Poland.
Magdalena WysockaDepartment of Molecular Biotechnology and Microbiology, Gdańsk University of Technology, ul. G. Narutowicza 11/12, 80-233, Gdańsk, Poland.
Marcin OlszewskiDepartment of Molecular Biotechnology and Microbiology, Gdańsk University of Technology, ul. G. Narutowicza 11/12, 80-233, Gdańsk, Poland. molszewski@pg.gda.pl.ORCID http://orcid.org/0000-0002-5116-2793
Gdańsk University of Technology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The DNA coding sequence of TaqStoffel polymerase was fused with the DNA-binding domain of Pyrococcus furiosus ligase. The resulting novel recombinant gene was cloned and expressed in E. coli. The recombinant enzyme was purified and its enzymatic features were studied. The fusion protein (PfuDBDlig-TaqS) was found to have enhanced processivity as a result of the conversion of the TaqDNA polymerase from a relatively low processive to a highly processive enzyme. The abovementioned processivity enhancement was about threefold as compared to the recombinant TaqStoffel DNA polymerase (TaqS), and the recombinant fusion protein was more thermostable. It had a half-life of 23 min at 99 °C as compared to 10 min for TaqS. The fusion protein also showed a significantly higher resistance to PCR inhibitors such as heparin or lactoferrin and the fusion polymerase-amplified GC-rich templates much more efficiently and was efficient even with 78% GC pairs.

Indexed as

Cloning, MolecularDNA-Binding ProteinsDNA-Directed DNA PolymeraseLigasesPolymerase Chain ReactionProtein DomainsPyrococcus furiosusRecombinant Fusion ProteinsDNA-Binding ProteinsDNA-Directed DNA PolymeraseLigasesRecombinant Fusion ProteinsArchaeonDNA polymeraseFusion DNA polymerasesPCR

Identifiers

PMID29103168
PMCPMC5756566
OpenAlexW2766013051

What OpenQuestion 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 OpenQuestion graph.