Evidence map›Paper›PMID 26884172›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

A protein constructed de novo enables cell growth by altering gene regulation.

Katherine M Digianantonio, Michael H Hecht

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Something from nothing: The birth of new phage defense genes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Emergence of antiphage functions from random sequence libraries reveals mechanisms of gene birth.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. De Novo Genes.Annual review of genetics · 2024
    Review
  7. Article
  8. Crystal structure and activity of a de novo enzyme, ferric enterobactin esterase Syn-F4.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Rescue ofeLife · 2023
    Article
  10. Article
  11. A de novo protein catalyzes the synthesis of semiconductor quantum dots.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Rigidifying aACS catalysis · 2021
    Article
  13. De novo proteins from random sequences through in vitro evolution.Current opinion in structural biology · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. mBio · 2019
    Article
  18. Review
  19. Review
  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

2 authors at 1 institution in 1 country.

Katherine M DigianantonioDepartment of Chemistry, Princeton University, Princeton, NJ 08540.
Michael H HechtDepartment of Chemistry, Princeton University, Princeton, NJ 08540 hecht@princeton.edu.
Princeton University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent advances in protein design rely on rational and computational approaches to create novel sequences that fold and function. In contrast, natural systems selected functional proteins without any design a priori. In an attempt to mimic nature, we used large libraries of novel sequences and selected for functional proteins that rescue Escherichia coli cells in which a conditionally essential gene has been deleted. In this way, the de novo protein SynSerB3 was selected as a rescuer of cells in which serB, which encodes phosphoserine phosphatase, an enzyme essential for serine biosynthesis, was deleted. However, SynSerB3 does not rescue the deleted activity by catalyzing hydrolysis of phosphoserine. Instead, SynSerB3 up-regulates hisB, a gene encoding histidinol phosphate phosphatase. This endogenous E. coli phosphatase has promiscuous activity that, when overexpressed, compensates for the deletion of phosphoserine phosphatase. Thus, the de novo protein SynSerB3 rescues the deletion of serB by altering the natural regulation of the His operon.

Indexed as

Gene Expression ProfilingBiocatalysisCulture MediaEscherichia coliEscherichia coli ProteinsHydrolysisOperonPhosphoric Monoester HydrolasesSOS Response, GeneticsTranscription, GeneticCulture MediaEscherichia coli ProteinsPhosphoric Monoester Hydrolasesphosphoserine phosphataseauxotrophde novo protein designhisBserBsynthetic biology

Identifiers

PMID26884172
PMCPMC4780649
OpenAlexW2275779322

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.