Evidence map›Paper›PMID 35788163›Full record

ArticleCommunications biology2022

Engineering of ultraID, a compact and hyperactive enzyme for proximity-dependent biotinylation in living cells.

Lea Kubitz, Sebastian Bitsch, Xiyan Zhao, Kerstin Schmitt, Lukas Deweid, Amélie Roehrig, Elisa Cappio Barazzone, Oliver Valerius, Harald Kolmar, Julien Béthune

Abstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing 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

89 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026
    Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

29 more citing papers are in PubMed but not listed here.

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

10 authors.

Lea Kubitz *Heidelberg University Biochemistry Center, Heidelberg, Germany.ORCID 0000-0003-4266-6591
Sebastian Bitsch *Institute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Darmstadt, Germany.
Xiyan Zhao *Heidelberg University Biochemistry Center, Heidelberg, Germany.
Kerstin SchmittInstitute of Microbiology and Genetics, Göttingen Center for Molecular Biosciences (GZMB) and Service Unit LCMS Protein Analytics, Georg-August-University Göttingen, Göttingen, Germany.ORCID 0000-0001-9627-031X
Lukas DeweidInstitute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Darmstadt, Germany.
Amélie RoehrigHeidelberg University Biochemistry Center, Heidelberg, Germany.
Elisa Cappio BarazzoneHeidelberg University Biochemistry Center, Heidelberg, Germany.
Oliver ValeriusInstitute of Microbiology and Genetics, Göttingen Center for Molecular Biosciences (GZMB) and Service Unit LCMS Protein Analytics, Georg-August-University Göttingen, Göttingen, Germany.ORCID 0000-0003-4430-819X
Harald KolmarInstitute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Darmstadt, Germany.
Julien BéthuneDepartment of Biotechnology, Hamburg University of Applied Sciences, Hamburg, Germany. Julien.bethune@haw-hamburg.de.ORCID 0000-0003-3673-3938

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proximity-dependent biotinylation (PDB) combined with mass spectrometry analysis has established itself as a key technology to study protein-protein interactions in living cells. A widespread approach, BioID, uses an abortive variant of the E. coli BirA biotin protein ligase, a quite bulky enzyme with slow labeling kinetics. To improve PDB versatility and speed, various enzymes have been developed by different approaches. Here we present a small-size engineered enzyme: ultraID. We show its practical use to probe the interactome of Argonaute-2 after a 10 min labeling pulse and expression at physiological levels. Moreover, using ultraID, we provide a membrane-associated interactome of coatomer, the coat protein complex of COPI vesicles. To date, ultraID is the smallest and most efficient biotin ligase available for PDB and offers the possibility of investigating interactomes at a high temporal resolution.

Indexed as

Carbon-Nitrogen LigasesEscherichia coli ProteinsBiotinBiotinylationEscherichia coliMass SpectrometryRepressor ProteinsBiotinbirA protein, E coliCarbon-Nitrogen LigasesEscherichia coli ProteinsRepressor Proteins

Identifiers

PMID35788163
PMCPMC9253107

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.